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<journal-meta>
<journal-id journal-id-type="publisher-id">Front. Microbiol.</journal-id>
<journal-title-group>
<journal-title>Frontiers in Microbiology</journal-title>
<abbrev-journal-title abbrev-type="pubmed">Front. Microbiol.</abbrev-journal-title>
</journal-title-group>
<issn pub-type="epub">1664-302X</issn>
<publisher>
<publisher-name>Frontiers Media S.A.</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="doi">10.3389/fmicb.2026.1752671</article-id>
<article-version article-version-type="Version of Record" vocab="NISO-RP-8-2008"/>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Review</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>Processing difficulties and biochemical barriers in camel milk fermentation</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author"><name><surname>Ali</surname> <given-names>Sifatun Nesa</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref>
<uri xlink:href="https://loop.frontiersin.org/people/3361433"/>
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</contrib>
<contrib contrib-type="author"><name><surname>Ayyash</surname> <given-names>Mutamed</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref>
<uri xlink:href="https://loop.frontiersin.org/people/1061730"/>
<role vocab="credit" vocab-identifier="https://credit.niso.org/" vocab-term="Writing &#x2013; review &#x0026; editing" vocab-term-identifier="https://credit.niso.org/contributor-roles/writing-review-editing/">Writing &#x2013; review &#x0026; editing</role>
</contrib>
<contrib contrib-type="author" corresp="yes"><name><surname>Kamal-Eldin</surname> <given-names>Afaf</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="aff" rid="aff2"><sup>2</sup></xref><xref ref-type="corresp" rid="c001"><sup>&#x002A;</sup></xref>
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<aff id="aff1"><label>1</label><institution>Department of Food Science, College of Agriculture and Veterinary Medicine, United Arab Emirates University</institution>, <city>Al Ain</city>, <country country="ae">United Arab Emirates</country></aff>
<aff id="aff2"><label>2</label><institution>National Water and Energy Center, United Arab Emirates University</institution>, <city>Al Ain</city>, <country country="ae">United Arab Emirates</country></aff>
<author-notes>
<corresp id="c001"><label>&#x002A;</label>Correspondence: Afaf Kamal-Eldin, <email xlink:href="mailto:afaf.kamal@uaeu.ac.ae">afaf.kamal@uaeu.ac.ae</email></corresp>
</author-notes>
<pub-date publication-format="electronic" date-type="pub" iso-8601-date="2026-02-02">
<day>02</day>
<month>02</month>
<year>2026</year>
</pub-date>
<pub-date publication-format="electronic" date-type="collection">
<year>2026</year>
</pub-date>
<volume>17</volume>
<elocation-id>1752671</elocation-id>
<history>
<date date-type="received">
<day>23</day>
<month>11</month>
<year>2025</year>
</date>
<date date-type="rev-recd">
<day>07</day>
<month>01</month>
<year>2026</year>
</date>
<date date-type="accepted">
<day>19</day>
<month>01</month>
<year>2026</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright &#x00A9; 2026 Ali, Ayyash and Kamal-Eldin.</copyright-statement>
<copyright-year>2026</copyright-year>
<copyright-holder>Ali, Ayyash and Kamal-Eldin</copyright-holder>
<license>
<ali:license_ref start_date="2026-02-02">https://creativecommons.org/licenses/by/4.0/</ali:license_ref>
<license-p>This is an open-access article distributed under the terms of the <ext-link ext-link-type="uri" xlink:href="https://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution License (CC BY)</ext-link>. The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p>
</license>
</permissions>
<abstract>
<p>Camel milk (CM) is recognized for its high nutritional enrichment, and the distinction from bovine milk mainly because of its unique protein composition, proteolytic products, and anti-microbial compounds. These unique chemical properties have positive effects on the nutritional value but negative impact on the sensory attributes and consumer acceptability of fermented CM. This review summarizes the current state of knowledge on CM fermentation, emphasizing the influence of milk composition on gel and microstructure formation, texture, and overall quality of the products. While the richness of fermented CM in bioactive peptides enhances its nutritional and therapeutic values, major challenges are associated with their thin consistency and weak gel structure. Various strategies to overcome these challenges and develop unique functional fermented CM products are discussed, including the use of alternative starter cultures (e.g., <italic>Lactobacillus helveticus, Lb. casei</italic>, and <italic>Lactiplantibacillus plantarum</italic>), stabilizing additives hydrocolloids or proteins, as well as optimized heat treatments, high-pressure processing and other emerging technologies. Despite several processing and formulation procedures, no particular approach has yet offered a comprehensive solution for achieving firm and stable camel yogurt. Therefore, it is important to accept fermented CM products as being different and develop means to improve their sensory quality and consumer acceptance. Overall, this review underscores the necessity for ongoing research to optimize the quality and commercial viability of fermented CM.</p>
</abstract>
<kwd-group>
<kwd>bovine milk yogurt</kwd>
<kwd>camel milk yogurt</kwd>
<kwd>fermentation</kwd>
<kwd>microstructure</kwd>
<kwd>starter cultures</kwd>
<kwd>texture</kwd>
</kwd-group>
<funding-group>
<award-group id="gs1">
<funding-source id="sp1">
<institution-wrap>
<institution>United Arab Emirates University</institution>
<institution-id institution-id-type="doi" vocab="open-funder-registry" vocab-identifier="10.13039/open_funder_registry">10.13039/501100006013</institution-id>
</institution-wrap>
</funding-source>
<award-id rid="sp1">12R137</award-id>
</award-group>
<funding-statement>The author(s) declared that financial support was received for this work and/or its publication. This research was funded by United Arab Emirates University grant number 12R137.</funding-statement>
</funding-group>
<counts>
<fig-count count="8"/>
<table-count count="5"/>
<equation-count count="0"/>
<ref-count count="186"/>
<page-count count="19"/>
<word-count count="15879"/>
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<custom-meta-group>
<custom-meta>
<meta-name>section-at-acceptance</meta-name>
<meta-value>Food Microbiology</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
<body>
<sec sec-type="intro" id="sec1">
<label>1</label>
<title>Introduction</title>
<p>The Middle East and North Africa along with some regions in Asia are major consumers of camel milk (CM) (<xref ref-type="bibr" rid="ref129">Muthukumaran et al., 2023</xref>). The worldwide camel population is estimated to be 32.7 million, with approximately 87.1% located in the Middle East and North Africa region (<xref ref-type="bibr" rid="ref135">Oselu et al., 2022a</xref>). Recently, CM has attracted broader global interest, including in Europe and North America, owing to its potential health benefits, including antidiabetic, anticancer, and hypoallergic properties (<xref ref-type="bibr" rid="ref127">Mullaicharam, 2014</xref>; <xref ref-type="bibr" rid="ref28">Benmeziane-Derradji, 2021</xref>; <xref ref-type="bibr" rid="ref122">Mohamed et al., 2021</xref>; <xref ref-type="bibr" rid="ref166">Swelum et al., 2021</xref>; <xref ref-type="bibr" rid="ref85">Kamal-Eldin et al., 2021</xref>; <xref ref-type="bibr" rid="ref73">Ho et al., 2022a</xref>; <xref ref-type="bibr" rid="ref10">Alia et al., 2023</xref>). However, unlike bovine milk (BM), CM consistently generates think and liquid-like fermented products (<xref ref-type="fig" rid="fig1">Figure 1</xref>). In particular, consumers typically opt for yogurts with dense texture and well-balanced viscous behavior but compared to BM yogurt, fermented camel milk is characterized by much lower hardness (52.5 vs. 11.8&#x202F;g) and viscosity (661 vs. 0.57&#x202F;Pa.sec) (<xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin, 2019</xref>). The microstructural properties, texture, and rheology of fermented dairy products, specifically yogurt and cheese, are of critical importance to their quality as primary determinants of appearance, mouthfeel, and overall consumer acceptability (<xref ref-type="bibr" rid="ref10">Alia et al., 2023</xref>). Thus, CM is more suitable for the manufacture of fermented drinkable product compared to BM yogurts (<xref ref-type="bibr" rid="ref161">Sobti et al., 2021</xref>; <xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>).</p>
<fig position="float" id="fig1">
<label>Figure 1</label>
<caption>
<p>Differences in appearance and consistency of fermented milk: <bold>(A)</bold> Fermented camel milk exhibiting a thin, pourable consistency with limited gel strength. <bold>(B)</bold> Bovine yogurt showing a firm, cohesive, and strong gel [reproduced from <xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin (2019)</xref> under creative commons permission].</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g001.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Panel (A) shows a spoon with liquid dripping from it into a bowl, indicating a pourable texture. Panel (B) displays a spoon lifting a thick, creamy substance from a container, suggesting a firmer consistency.</alt-text>
</graphic>
</fig>
<p>These differences between fermented CM and BM products have been attributed to several factors, including its unique chemical composition, complex colloidal system, protein micelle and fat globule sizes, and antimicrobial compounds (<xref ref-type="bibr" rid="ref122">Mohamed et al., 2021</xref>; <xref ref-type="bibr" rid="ref121">Mohamed et al., 2020</xref>; <xref ref-type="bibr" rid="ref123">Mohamed et al., 2022a</xref>; <xref ref-type="bibr" rid="ref115">Mbye et al., 2022</xref>; <xref ref-type="bibr" rid="ref16">Arain et al., 2023a</xref>; <xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>). Comparison of the microstructures of CM and BM-acid gels revealed a denser casein network in BM than in CM because the smaller size of the casein micelles in the latter result in greater bonding during acidification (<xref ref-type="bibr" rid="ref62">Glantz et al., 2010</xref>). The relatively low level of <italic>&#x03BA;</italic>-casein, lack of <italic>&#x03B2;</italic>-lactoglobulin, high &#x03B2;-casein content, and large casein micelles are considered to contribute to the poor coagulation leading to the weak structure, and thin consistency of fermented CM products compared to fermented BM products (<xref ref-type="bibr" rid="ref73">Ho et al., 2022a</xref>; <xref ref-type="bibr" rid="ref132">O&#x2019;Kennedy et al., 2006</xref>).</p>
<p>The formation of fermented CM may be facilitated with the use of certain additives such as citrate that can dissociate the micelles into monomers, leading to improvement to the texture of the CM gel (<xref ref-type="bibr" rid="ref175">Wang J. et al., 2025</xref>). The nutritional value and consumer perception of these products can also be enhanced by adding additional proteins (<xref ref-type="bibr" rid="ref105">Lesme et al., 2020</xref>), hydrocolloids (<xref ref-type="bibr" rid="ref148">Saleh et al., 2018</xref>), and/or fruit pulp (<xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>). In addition, new technologies, optimization of processing and fermentation conditions, and the use of stabilizers or fortifications could help overcome these challenges (<xref ref-type="bibr" rid="ref17">Arain et al., 2023b</xref>). Although extensive studies have been conducted on creating various fermented BM products with flavorings, colorants, and sweeteners; however, similar investigations on fermented CM products remain limited (<xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>).</p>
<p>Several reviews have emphasized the hypoallergenic, anticarcinogenic, and antimicrobial properties of CM, along with its potential application in the development of functional and probiotic foods (<xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>; <xref ref-type="bibr" rid="ref14">Ansari et al., 2024</xref>; <xref ref-type="bibr" rid="ref11">Almasri et al., 2024</xref>; <xref ref-type="bibr" rid="ref114">Marete et al., 2024</xref>; <xref ref-type="bibr" rid="ref152">Seyiti et al., 2024</xref>). In addition to the health-promoting aspects, the global status, production trends, and economic value chain of the CM industry have been detailed, identifying both market opportunities and operational challenges (<xref ref-type="bibr" rid="ref7">Ait El Alia et al., 2025</xref>). The high nutritional and therapeutic value of fermented CM products has generated great interest in understanding the reasons contributing to their weak gels and watery consistency in order to find appropriate strategies to overcome these challenges (<xref ref-type="bibr" rid="ref28">Benmeziane-Derradji, 2021</xref>; <xref ref-type="bibr" rid="ref122">Mohamed et al., 2021</xref>; <xref ref-type="bibr" rid="ref166">Swelum et al., 2021</xref>; <xref ref-type="bibr" rid="ref73">Ho et al., 2022a</xref>; <xref ref-type="bibr" rid="ref10">Alia et al., 2023</xref>). The aim of this review is to synthesize and extend this current knowledge by focusing on the properties of fermented CM products and how they are affected by the chemical composition of the milk, fermentation bacteria, processing conditions, and stabilizing agents. This knowledge is essential for the further design of strategies that will facilitate the production of nutritional and therapeutic fermented CM products with improved consumer acceptance.</p>
</sec>
<sec id="sec2">
<label>2</label>
<title>Chemical and structural transformations during fermentation</title>
<p>The yogurt fermentation process is preceded by heat treatment to facilitate the formation of complex networks between the soluble whey proteins and <italic>&#x03BA;</italic>-casein through thiol/disulfide bond interchanges (<xref ref-type="bibr" rid="ref19">Asaduzzaman et al., 2021</xref>). Heating milk prior to fermentation affects the degree of whey protein denaturation and the formation of micelle-bound and soluble complexes with <italic>&#x03BA;</italic>-casein (<xref ref-type="bibr" rid="ref13">Anema, 2021</xref>). The micelle-bound complexes are responsible for increasing the final firmness of acid gels, while the soluble complexes enhance the water-holding capacity and firmness of yogurt gels (<xref ref-type="bibr" rid="ref19">Asaduzzaman et al., 2021</xref>). However, the contributions of the abundance and chemical constitution of denatured whey protein/<italic>&#x03BA;</italic>-casein complexes to the gelation processes and the textural properties of the heated milk and final products remain unclear (<xref ref-type="bibr" rid="ref45">Donato et al., 2007</xref>). Nevertheless, it is known that the milk type along with the heating and fermentation treatments themselves significantly impact the properties of yogurt gels, mainly the microstructure, firmness, rheology, water-holding capacity, and whey separation (<xref ref-type="bibr" rid="ref113">Mahomud et al., 2017</xref>).</p>
<p>Heating of BM above 70&#x202F;&#x00B0;C cause denaturation of <italic>&#x03B2;</italic>-lactoglobulin, the major whey protein in the milk, thereby exposing its free thiol (-SH) group (<xref ref-type="bibr" rid="ref112">Mahomud et al., 2021</xref>). The thiol/disulfide exchange reactions between the free thiol group (-SH) of denatured &#x03B2;-lactoglobulin and the S-S bonds of <italic>&#x03BA;</italic>-casein in BM are well-documented (<xref ref-type="bibr" rid="ref19">Asaduzzaman et al., 2021</xref>; <xref ref-type="bibr" rid="ref113">Mahomud et al., 2017</xref>). The formation of intermolecular S-S bridges through covalent bonds and hydrophobic interactions occurring at temperatures below 75&#x202F;&#x00B0;C depends on the <italic>&#x03B2;</italic>-lactoglobulin concentration (<xref ref-type="bibr" rid="ref113">Mahomud et al., 2017</xref>). These intermolecular thiol/disulfide interchange reactions during heating and subsequent acidification result in covalent bonds that improve the microstructure (<xref ref-type="bibr" rid="ref57">Gazi and Huppertz, 2015</xref>) and enhance the strength of yogurt gels (<xref ref-type="bibr" rid="ref112">Mahomud et al., 2021</xref>). Unlike <italic>&#x03B2;</italic>-lactoglobulin, <italic>&#x03B1;</italic>-lactalbumin, as the major whey protein in CM, has no free thiol group and therefore cannot initiate thiol/disulfide exchange reactions. However, these reactions can be initiated by camel serum albumin or other whey proteins, enabling <italic>&#x03B1;</italic>-lactalbumin to cross-link with the micellar caseins in CM. Another difference between &#x03B1;-lactalbumin and <italic>&#x03B2;</italic>-lactoglobulin is that the former readily forms a molten globule, an intermediate between the native and completely denatured form of the protein, under even mild denaturation conditions (<xref ref-type="bibr" rid="ref139">Permyakov, 2020</xref>). The low concentration of <italic>&#x03BA;</italic>-casein in CM is another factor that may affect the formation and concentration of the whey protein/&#x03BA;-casein complex.</p>
<p>Bacterial fermentation gradually reduces the milk pH. Once the pH reaches the isoelectric point of caseins (pH 4.3 for CM and pH 4.6 for BM), the casein micelles are destabilized owing to a decrease in their net negative charges, electrostatic repulsions, and steric stabilization (<xref ref-type="bibr" rid="ref116">Meletharayil et al., 2015</xref>). As shown in <xref ref-type="fig" rid="fig2">Figure 2</xref>, this destabilization leads to the coagulation of caseins and the formation of three-dimensional gel networks, influenced by the milk protein complexes (<xref ref-type="bibr" rid="ref15">Arab et al., 2023</xref>). The -SH/S-S interchange reactions in the micelle-bound whey proteins continue to form during acidification (pH&#x202F;&#x003C;&#x202F;~6.7), leading to an increase in the gel&#x2019;s storage modulus (G&#x2032;) (<xref ref-type="bibr" rid="ref113">Mahomud et al., 2017</xref>) and the final elastic properties of the yogurt (<xref ref-type="bibr" rid="ref186">Zhao et al., 2021</xref>). The soluble whey protein/<italic>&#x03BA;</italic>-casein complexes also play a critical role in the structural characteristics of acid gels (<xref ref-type="bibr" rid="ref113">Mahomud et al., 2017</xref>; <xref ref-type="bibr" rid="ref99">Lakemond and van Vliet, 2008</xref>; <xref ref-type="bibr" rid="ref38">Chever et al., 2014</xref>). During acidification, some casein micelles may disintegrate due to the solubilization of colloidal calcium phosphate (<xref ref-type="bibr" rid="ref156">Sinaga et al., 2016</xref>). This process decreases the overall negative charge and electrostatic repulsion while enhancing hydrophobic attractions between micelles. Consequently, the storage modulus (G&#x2032;) of the yogurt elevates, encouraging protein aggregation, linkage formation, and expansion of the protein network (<xref ref-type="bibr" rid="ref131">Nguyen et al., 2018</xref>).</p>
<fig position="float" id="fig2">
<label>Figure 2</label>
<caption>
<p>Schematic representation of the protein network formed in yogurt gels by the pre-fermentation heat treatment and acidification by bacterial cultures. Heating causes whey protein (WP) to denature and to form soluble and micelle-bound WP&#x2013;<italic>&#x03BA;</italic>-casein (WP/&#x03BA;-CN) complexes via thiol&#x2013;disulfide (&#x2013;S&#x2013;S&#x2013;) interactions. Subsequent acidification to the isoelectric point of milk reduces electrostatic repulsion between the casein micelles and promote their aggregation, resulting in the formation of a protein gel network characterized by interconnected aggregates, strands, and voids typical of yogurt structure [adapted from <xref ref-type="bibr" rid="ref19">Asaduzzaman et al. (2021)</xref> and <xref ref-type="bibr" rid="ref113">Mahomud et al. (2017)</xref>].</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g002.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Diagram showing the formation of protein gel networks in yogurt. Casein micelles with electrostatic repulsion and &#x03BA;-casein undergo heating. This forms micellar WP/&#x03BA;-CN complexes in heated milk gel at pH 6.7. Acidification leads to isoelectric conditions, forming aggregates with voids and strands in acid milk gel at pH 4.6.</alt-text>
</graphic>
</fig>
<p>The microstructure of yogurt is based on a casein matrix consisting of strands, aggregates, and voids (<xref ref-type="fig" rid="fig3">Figure 3</xref>) (<xref ref-type="bibr" rid="ref140">Prasanna et al., 2018</xref>). Fermentation transforms milk from a Newtonian fluid to a semi-solid gel, in which the created protein network retains liquid in the voids or pores (<xref ref-type="bibr" rid="ref15">Arab et al., 2023</xref>). Polymerized whey proteins and whey protein&#x2013; <italic>&#x03BA;</italic>-casein complexes fill these voids, leading to more compact microstructures in BM (<xref ref-type="bibr" rid="ref29">Bierzu&#x0144;ska et al., 2019</xref>; <xref ref-type="bibr" rid="ref52">Fang and Guo, 2019</xref>). However, in the fermented CM hydrogel, these voids can retain water, resulting in less syneresis (whey separation) compared to that occurring in BM under the same conditions. The network responsible for water retention or expulsion is determined by the cross-linked protein matrix and clusters of casein micelles with distinct globular forms, as well as the polysaccharides and fat globules contained within the yogurt&#x2019;s microstructure (<xref ref-type="bibr" rid="ref15">Arab et al., 2023</xref>; <xref ref-type="bibr" rid="ref94">Kim et al., 2020</xref>). Syneresis occurs in bovine yogurt as a result of physicochemical changes that cause gel shrinkage, signifying the release of bound whey from the continuous network (<xref ref-type="bibr" rid="ref104">Lee and Lucey, 2010</xref>). Syneresis is regulated through two groups of factors: (1) factors influencing water-holding capacity, including physical network density, formation, stability, and chemical water elimination; and (2) factors enhancing water removal from networks, including intra-network stresses (rearrangement, fast cooling, acidification) and extra-network stresses (<xref ref-type="bibr" rid="ref15">Arab et al., 2023</xref>). Understanding yogurt microstructures can therefore help to determine the degree of compact cluster formation and syneresis (<xref ref-type="bibr" rid="ref164">Sobti et al., 2020</xref>). For a yogurt to resist syneresis, it is essential to maintain appropriate gel stiffness and water-holding capacity (<xref ref-type="bibr" rid="ref61">Gilbert et al., 2020</xref>). Bovine yogurt typically has smaller voids due to the highly aggregated protein clusters, whereas camel yogurt has larger voids in its microstructure with great water-holding capacity (<xref ref-type="bibr" rid="ref164">Sobti et al., 2020</xref>). Owing to the absence of gel stiffness, stirred yogurt can also undergo less syneresis compared to set yogurt (<xref ref-type="bibr" rid="ref15">Arab et al., 2023</xref>). Water retention in the voids makes fermented CM softer, more elastic, and more liquid (<xref ref-type="bibr" rid="ref73">Ho et al., 2022a</xref>; <xref ref-type="bibr" rid="ref132">O&#x2019;Kennedy et al., 2006</xref>). Despite the lower degree of syneresis in camel than bovine yogurt, the shrinkage of the gel structure renders the camel gel more susceptible to delayed and increased syneresis during storage or handling (<xref ref-type="bibr" rid="ref136">Oselu et al., 2022b</xref>). Indeed, the syneresis index of BM yogurt decreases considerably during storage when CM is added, indicating an increase in the water-holding capacity (<xref ref-type="bibr" rid="ref84">Kamal-Eldin et al., 2020</xref>).</p>
<fig position="float" id="fig3">
<label>Figure 3</label>
<caption>
<p>Differences in the microstructures of yogurt gels formed from caseins: <bold>(A)</bold> Fermented camel milk gel exhibiting a loose, heterogenous network characterized by elongated protein strands and large voids, and <bold>(B)</bold> fermented bovine milk gel displaying a compact, homogenous protein network with smaller pores and higher structural continuity. The fermented camel milk is characterized by elongated strands and large voids, while the bovine milk provides a denser structure [reproduced from <xref ref-type="bibr" rid="ref175">Wang et al. (2025)</xref> under creative commons permission].</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g003.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">(A) High-magnification electron micrograph showing a complex network of fibrous structures with various pore sizes. (B) Similar micrograph highlighting a more uniform distribution of smaller pores. Both images are labeled with magnification and scale bar details.</alt-text>
</graphic>
</fig>
<p>Exopolysaccharides (EPS), produced during bacterial fermentation of milk, play crucial roles in yogurt quality by influencing the gelling, stabilizing, thickening, and water-binding abilities; preventing syneresis; and improving texture without compromising sensorial attributes (<xref ref-type="bibr" rid="ref117">Mende et al., 2016</xref>). EPS also exhibit functional properties such as antioxidant activity, prebiotic benefits, and immunomodulatory effects (<xref ref-type="bibr" rid="ref145">Riaz Rajoka et al., 2020</xref>). Charged EPS bind to protein networks, while uncharged EPS accumulate in the serum, causing thermodynamic incompatibilities (<xref ref-type="bibr" rid="ref100">Laneuville and Turgeon, 2014</xref>). EPS affect the stability of yogurt by interacting with caseins, whey proteins, bacterial cells, and minerals, affecting complexation, co-solubility, or incompatibility (<xref ref-type="bibr" rid="ref117">Mende et al., 2016</xref>). Negatively charged EPS induce repulsive interactions, whereas neutral EPS promote phase separation (<xref ref-type="bibr" rid="ref67">Han et al., 2023</xref>). Yogurt with EPS-producing strains has higher consistency but lower yield stress, elastic modulus, and viscosity due to the EPS forming channels that decrease protein interactions and prevent syneresis (<xref ref-type="bibr" rid="ref69">Hassan et al., 2003</xref>). <italic>Lactobacillus delbrueckii</italic> ssp<italic>. bulgaricus</italic> and <italic>Streptococcus thermophilus</italic> are key EPS producers, which are known to enhance a BM yogurt&#x2019;s viscosity and sensory attributes (<xref ref-type="bibr" rid="ref170">Tiwari et al., 2021</xref>) through cross-feeding and promoting metabolites exchange (<xref ref-type="bibr" rid="ref108">Liu et al., 2016</xref>).</p>
<p>During fermentation, lactic acid bacteria (LAB) release enzymes that metabolize milk components through glycolysis, proteolysis, and lipolysis, producing lactic acid, other organic acids, peptides, and free amino and fatty acids, which influence the yogurt&#x2019;s flavor and texture (<xref ref-type="fig" rid="fig4">Figure 4</xref>) (<xref ref-type="bibr" rid="ref158">Smid and Kleerebezem, 2014</xref>; <xref ref-type="bibr" rid="ref30">Bintsis, 2018</xref>; <xref ref-type="bibr" rid="ref72">Hayek and Ibrahim, 2013</xref>). Along with glycolysis and lipolysis, proteolysis is a crucial process in the production and development of fermented dairy products given its major impact on texture and flavor. The generated amino acids and peptides function as precursors for other catabolic processes that produce both desirable and undesirable flavors and odors (<xref ref-type="bibr" rid="ref154">Shori, 2017</xref>), playing major roles in the bioactivities of fermented products. Proteolysis, caused by <italic>Lactobacillus</italic> spp., affects the texture and aroma of yogurt made from fermented CM and negatively affects the rheological parameters during storage (<xref ref-type="bibr" rid="ref56">Gandhi and Shah, 2014</xref>). Yogurts may shear thin when there is an increase in total solids due to elevated proteolytic activity (<xref ref-type="bibr" rid="ref1">Abd El-Aziz et al., 2022</xref>; <xref ref-type="bibr" rid="ref40">Costa et al., 2022</xref>). Differences in buffering capacity, proteolytic activity, and antimicrobial proteins contribute to observed variations in acidity between the fermented products prepared from CM and BM (<xref ref-type="bibr" rid="ref161">Sobti et al., 2021</xref>). The proteolytic systems of LAB significantly impact protein, peptide, and amino acid availability for growth and the final rheological and sensory properties of fermented foods (<xref ref-type="bibr" rid="ref72">Hayek and Ibrahim, 2013</xref>). Caseins are the primary substrates for LAB proteolytic systems during fermentation and storage, as evidenced by reduced electrophoretic band intensities for <italic>&#x03BA;</italic>-, <italic>&#x03B2;</italic>-, and <italic>&#x03B1;</italic>-caseins (<xref ref-type="bibr" rid="ref107">Li et al., 2019</xref>), while the whey proteins &#x03B1;-lactalbumin and &#x03B2;-lactoglobulin remain largely unaffected (<xref ref-type="bibr" rid="ref63">Gonz&#x00E1;lez-Olivares et al., 2014</xref>). By producing essential growth factors such as peptides and amino acids, proteolysis may have an influence on the ability of probiotics to survive and thrive in fermented dairy products (<xref ref-type="bibr" rid="ref169">Tavakoli et al., 2019</xref>; <xref ref-type="bibr" rid="ref35">Chelladhurai et al., 2024</xref>). LAB strains such <italic>Lactiplantibacillus plantarum</italic> influence the proteolysis of milk when co-fermented with <italic>S. thermophilus</italic> during cold storage (<xref ref-type="bibr" rid="ref107">Li et al., 2019</xref>), and these strains also impact the structure, nutritional profile, and functional properties of both fermented CM and BM (<xref ref-type="bibr" rid="ref80">Imen et al., 2015</xref>). Use of a combination of <italic>Lactobacillus helveticus</italic> and <italic>L. plantarum</italic> strains improved BM protein degradation and decreased protein antigenicity (<xref ref-type="bibr" rid="ref186">Zhao et al., 2021</xref>).</p>
<fig position="float" id="fig4">
<label>Figure 4</label>
<caption>
<p>Overview of general metabolic pathways used by lactic acid bacteria (LAB) during milk fermentation. Carbohydrate, protein, and lipid metabolism by LAB leads to the production of key flavor compounds, including organic acids, alcohols, aldehydes, ketones, and sulphur containing compounds [adapted from <xref ref-type="bibr" rid="ref76">Hu et al. (2022)</xref>] with permission from Taylor &#x0026; Francis.</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g004.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Flowchart illustrating the metabolic pathways of complex carbohydrates, citrate, proteins, and lipids. Monosaccharides convert to pyruvate, ethanol, acetic acid, and lactic acid. Citrate and proteins form free amino acids, leading to various acid and alcohol products. Lipids transform to free fatty acids, yielding acetyl CoA, thiols, and other compounds through oxidation and enzyme reactions. Key processes like hydrolases, dehydrogenase, and oxidation are highlighted.</alt-text>
</graphic>
</fig>
</sec>
<sec id="sec3">
<label>3</label>
<title>Key factors affecting camel yogurt quality</title>
<sec id="sec4">
<label>3.1</label>
<title>Milk composition and characteristics</title>
<p><xref ref-type="table" rid="tab1">Table 1</xref> compares the chemical composition of CM and BM and shows major differences in the relative casein proportions and micelle properties. CM is very different from BM, including the paler (whitish) color, slightly salty flavor, and lower density (1.029&#x202F;g/mL) (<xref ref-type="bibr" rid="ref81">Izadi et al., 2019</xref>). The distinct composition of CM results in a relatively weaker response to traditional gel production methods used with BM, such lactic acid fermentation or renin treatments (<xref ref-type="bibr" rid="ref20">Attia et al., 2001</xref>). Because texture has a major impact on sensory and quality parameters such as mouth feel, appearance, and customer acceptance, the poor coagulation properties of CM render commercial fermented CM products, including yogurt and cheese, with generally low acceptance by consumers (<xref ref-type="bibr" rid="ref138">Patel et al., 2022</xref>). Although stabilizers, skim milk powder, calcium chloride, and commercial yogurt culture have been used in a series of initiatives to produce high-quality yogurt from CM, the texture and consistency of the gels remain undesirable (<xref ref-type="bibr" rid="ref12">Al-Zoreky and Al-Otaibi, 2015</xref>). Another disadvantage is that the fermentation of CM generally takes longer than required for BM fermentation (<xref ref-type="bibr" rid="ref55">Galeboe et al., 2018</xref>). Therefore, further research is needed to optimize the operating parameters and standardize procedures to improve the production process and acceptability of fermented CM (<xref ref-type="bibr" rid="ref151">Seifu, 2023</xref>).</p>
<table-wrap position="float" id="tab1">
<label>Table 1</label>
<caption>
<p>Chemical composition of proteins, fats, lipids in camel and bovine milk.</p>
</caption>
<table frame="hsides" rules="groups">
<thead>
<tr>
<th align="left" valign="top">Components</th>
<th align="center" valign="top">Camel milk</th>
<th align="center" valign="top">Bovine milk</th>
<th align="left" valign="top">Reference</th>
</tr>
</thead>
<tbody>
<tr>
<td align="left" valign="top">Protein (%)</td>
<td align="center" valign="top">3.1</td>
<td align="center" valign="top">3.4</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref121">Mohamed et al. (2020)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Total caseins content (%)</td>
<td align="center" valign="top">50&#x2013;88</td>
<td align="center" valign="top">80&#x2013;84</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref121">Mohamed et al. (2020)</xref> and <xref ref-type="bibr" rid="ref51">Fabiano et al. (2013)</xref></td>
</tr>
<tr>
<td align="left" valign="top">&#x03B1;S1-, <italic>&#x03B1;</italic>S2-, &#x03B2;-, &#x03BA;-caseins (relative %)</td>
<td align="center" valign="top">26:4:67:3</td>
<td align="center" valign="top">38:10:36:12</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref121">Mohamed et al. (2020)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Casein micelle&#x2019;s diameter size (nm)</td>
<td align="center" valign="top">20&#x2013;300</td>
<td align="center" valign="top">40&#x2013;160</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref137">Park and Haenlein (2013)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Whey proteins (WP) (%)</td>
<td align="center" valign="top">20&#x2013;25</td>
<td align="center" valign="top">18&#x2013;20</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref121">Mohamed et al. (2020)</xref> and <xref ref-type="bibr" rid="ref51">Fabiano et al. (2013)</xref></td>
</tr>
<tr>
<td align="left" valign="top">&#x03B2;-lactoglobulin (% of WP)</td>
<td align="center" valign="top">-</td>
<td align="center" valign="top">53.6</td>
<td align="left" valign="top" rowspan="5"><xref ref-type="bibr" rid="ref174">Tsermoula et al. (2021)</xref>, <xref ref-type="bibr" rid="ref174">Tsermoula et al. (2021)</xref>, <xref ref-type="bibr" rid="ref123">Mohamed et al. (2022a)</xref>, <xref ref-type="bibr" rid="ref64">Hailu et al. (2016)</xref>, and <xref ref-type="bibr" rid="ref64">Hailu et al. (2016)</xref></td>
</tr>
<tr>
<td align="left" valign="top">&#x03B1;-lactalbumin (% of WP)</td>
<td align="center" valign="top">27</td>
<td align="center" valign="top">20.1</td>
</tr>
<tr>
<td align="left" valign="top">Lactoferrin (&#x03BC;g/mL)</td>
<td align="center" valign="top">639&#x2013;210</td>
<td align="center" valign="top">76.7&#x2013;140</td>
</tr>
<tr>
<td align="left" valign="top">Serum albumin (%)</td>
<td align="center" valign="top">26</td>
<td align="center" valign="top">6.2</td>
</tr>
<tr>
<td align="left" valign="top">Immunoglobulins A, G, &#x0026; M (g/l)</td>
<td align="center" valign="top">1.5 (18%)</td>
<td align="center" valign="top">0.3 (5.3%)</td>
</tr>
<tr>
<td align="left" valign="top">Fat (%)</td>
<td align="center" valign="top">2.9&#x2013;5.4</td>
<td align="center" valign="top">3.7&#x2013;4.4</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref157">Singh et al. (2017)</xref> and <xref ref-type="bibr" rid="ref79">Imamou Hassani et al. (2022)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Dry matter of cholesterol (mg/100&#x202F;g)</td>
<td align="center" valign="top">37.15</td>
<td align="center" valign="top">25.63</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref95">Konuspayeva and Faye (2021)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Triacylglycerols (%)</td>
<td align="center" valign="top">96</td>
<td align="center" valign="top">&#x003E;98%</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref50">Ereifej et al. (2011)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Branched-chain fatty acids (%)</td>
<td align="center" valign="top">3.03</td>
<td align="center" valign="top">1.82</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref46">Dreiucker and Vetter (2011)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Fat globule&#x2019;s diameter size (&#x03BC;m)</td>
<td align="center" valign="top">3.2&#x2013;5.6</td>
<td align="center" valign="top">4.3&#x2013;8.4</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref91">Khalesi et al. (2017)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Lactose (%)</td>
<td align="center" valign="top">4.5</td>
<td align="center" valign="top">4.7</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref122">Mohamed et al. (2021)</xref>
</td>
</tr>
</tbody>
</table>
</table-wrap>
<p>In a previous study, conducted by our research team, showed that the properties of fermented CM and BM are affected by the milk type, bacteria, temperature, and their interactions (<xref ref-type="bibr" rid="ref35">Chelladhurai et al., 2024</xref>). Compared to BM, CM is void of <italic>&#x03B2;</italic>-lactoglobulin, has lower <italic>&#x03BA;</italic>-casein and higher &#x03B2;-casein contents, has larger casein micelles, smaller fat globules, and higher levels of proteolytic products (<xref ref-type="bibr" rid="ref121">Mohamed et al., 2020</xref>; <xref ref-type="bibr" rid="ref115">Mbye et al., 2022</xref>; <xref ref-type="bibr" rid="ref35">Chelladhurai et al., 2024</xref>; <xref ref-type="bibr" rid="ref174">Tsermoula et al., 2021</xref>). As discussed above (<xref ref-type="fig" rid="fig2">Figure 2</xref>), <italic>&#x03B2;</italic>-lactoglobulin and <italic>&#x03BA;</italic>-casein play a very important role in yogurt quality. The size of casein micelles in CM (20&#x2013;300&#x202F;nm) is two-folds larger than that of the micelles in BM (40&#x2013;160&#x202F;nm) (<xref ref-type="bibr" rid="ref166">Swelum et al., 2021</xref>), which may potentially influence the final texture and consistency of fermented CM. Differences in protein profiles and amino acid sequences between CM and BM can also significantly influence the composition of their fermented products (<xref ref-type="bibr" rid="ref81">Izadi et al., 2019</xref>). The relative composition of <italic>&#x03B1;</italic>S1-, &#x03B1;S2-, <italic>&#x03B2;</italic>-, and <italic>&#x03BA;</italic>-caseins in CM was found to be 26:4:67:3 compared to a ratio of 38:10:36:12 in BM (<xref ref-type="bibr" rid="ref121">Mohamed et al., 2020</xref>). This difference results in higher concentrations of &#x03B2;-casein and lower levels of &#x03B1;-caseins in CM. Furthermore, CM lacks &#x03B2;-lactoglobulin and has lower levels of &#x03BA;-casein (3.5%) than BM (10%), which are the two most important proteins for the initial formation of yogurt gels (<xref ref-type="bibr" rid="ref123">Mohamed et al., 2022a</xref>). Moreover, CM exhibits a higher content of whey proteins (20&#x2013;25%) than BM (18&#x2013;20%) (<xref ref-type="bibr" rid="ref121">Mohamed et al., 2020</xref>; <xref ref-type="bibr" rid="ref51">Fabiano et al., 2013</xref>). Together, these variations contribute to differences in the ultimate rheological properties of fermented CM, such as weaker coagulation and gel structure, from those of BM yogurt (<xref ref-type="bibr" rid="ref64">Hailu et al., 2016</xref>).</p>
<p>A crucial factor that affects the fermentability of CM and BM is the degree of proteolysis of the milk proteins by the bacteria and indigenous factors (<xref ref-type="bibr" rid="ref35">Chelladhurai et al., 2024</xref>). CM shows a higher degree of proteolysis than BM, which correlates negatively to the bacterial count (<xref ref-type="fig" rid="fig5">Figure 5</xref>). In addition, <italic>&#x03B2;</italic>-casein, which is highly abundant in CM, is more susceptible to proteolysis than the other caseins. CM contains shorter &#x03B2;-casein chains with more proline residues, and its hydrolysis produces bioactive peptides and releases antioxidative amino acids such as phenylalanine and tryptophan (<xref ref-type="bibr" rid="ref81">Izadi et al., 2019</xref>). Such an increase in proteolytic products enhances the water holding capacity and the watery consistency of Fermented CM and influences the gel&#x2019;s internal stability (<xref ref-type="bibr" rid="ref2">Abdeldaiem et al., 2022</xref>).</p>
<fig position="float" id="fig5">
<label>Figure 5</label>
<caption>
<p>Principal component analysis showing the effect of milk type on the chemical properties of fermented camel and bovine milk. The upper panel <bold>(A)</bold> shows the loading plot (TA&#x202F;=&#x202F;titratable acidity; OPA&#x202F;=&#x202F;proteolytic products) and the lower panel <bold>(B)</bold> shows the score plot for camel and bovine milk [reproduced from <xref ref-type="bibr" rid="ref35">Chelladhurai et al. (2024)</xref> with permission from Elsevier].</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g005.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Principal Component Analysis (PCA) graphs are shown. Panel A depicts vectors for pH, lactose concentration, lactic acid concentration, bacterial count, OPA, and TA, plotted on axes of PC1 (58.7%) and PC2 (16.9%). Panel B displays a scatter plot differentiating cow milk (red) and camel milk (blue) based on PC1 and PC2 axes.</alt-text>
</graphic>
</fig>
<p>CM exhibits antimicrobial activities that may affect bacterial growth during fermentation (<xref ref-type="bibr" rid="ref166">Swelum et al., 2021</xref>; <xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>). CM significantly surpasses BM in serum albumin content (26% vs. 6.2%) (<xref ref-type="bibr" rid="ref115">Mbye et al., 2022</xref>) and in the contents of immunoglobulins A, G, and M (18% <italic>vs</italic> 3.5%) (<xref ref-type="bibr" rid="ref64">Hailu et al., 2016</xref>). Moreover, CM is significantly richer in lactoferrin and lysozyme compared to BM (639.4&#x2013;2094.9&#x202F;&#x03BC;g/mL <italic>vs</italic> 76.7&#x2013;140&#x202F;&#x03BC;g/mL), making it more potent in immune defense and antimicrobial activities (<xref ref-type="bibr" rid="ref47">El-Agamy, 2000</xref>; <xref ref-type="bibr" rid="ref87">Kappeler et al., 1998</xref>). The lactoferrin in CM has been shown to exhibit antibacterial, antiviral, anticancer, anti-inflammatory, and immunomodulatory effects. Similarly, CM contains higher levels of lysozyme, in the range of 23.3&#x2013;71.4&#x202F;&#x03BC;g/mL compared to only 7&#x202F;&#x03BC;g/mL lactoferrin found in BM (<xref ref-type="bibr" rid="ref48">Elagamy et al., 1996</xref>). This elevated lysozyme concentration enhances CM&#x2019;s antibacterial properties, further contributing to its potential health benefits (<xref ref-type="bibr" rid="ref123">Mohamed et al., 2022a</xref>). These notable differences in protein composition might contribute to a denser texture of CM compared to BM.</p>
<p>In casein micelles, calcium binds to &#x03B1;S1-, &#x03B1;S2-, and <italic>&#x03B2;</italic>-caseins in the core, while <italic>&#x03BA;</italic>-casein forms a &#x201C;brush&#x201D; on the micelle surface (<xref ref-type="bibr" rid="ref43">de Kruif and Zhulina, 1996</xref>; <xref ref-type="bibr" rid="ref42">Dalgleish and Corredig, 2012</xref>). CM caseins are characterized by lower degree of phosphorylation and micelle stability compared to those of BM (<xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin, 2019</xref>; <xref ref-type="bibr" rid="ref147">Ryskaliyeva et al., 2018</xref>; <xref ref-type="bibr" rid="ref97">Kumar et al., 2015</xref>). The higher levels of &#x03B2;-casein and their greater chaperone activity in CM compared to BM (<xref ref-type="bibr" rid="ref97">Kumar et al., 2015</xref>) can further increase the amphiphilicity and detergent-like properties of CM proteins, which impairs their aggregation and refolding (<xref ref-type="bibr" rid="ref144">Raynes et al., 2015</xref>). In addition, the structure and properties of fermented CM were improved by adding bovine casein and whey proteins (<xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin, 2019</xref>).</p>
<p>The functional properties of fermented CM may also be affected by the milk lipids. Compared to BM, CM exhibits a slightly higher fat content (<xref ref-type="table" rid="tab1">Table 1</xref>) and smaller fat globule size (<xref ref-type="bibr" rid="ref91">Khalesi et al., 2017</xref>), which may be linked to the slower and more thorough creaming process (<xref ref-type="bibr" rid="ref101">Lean, 2011</xref>). In particular, CM has a higher concentration of branched-chain fatty acids (3.03%) than BM (1.82%) (<xref ref-type="bibr" rid="ref46">Dreiucker and Vetter, 2011</xref>) and also has a markedly lower carotene content (<xref ref-type="bibr" rid="ref39">Claeys et al., 2014</xref>). These differences result in a &#x201C;waxy texture&#x201D; and whiter color of fermented CM (<xref ref-type="bibr" rid="ref50">Ereifej et al., 2011</xref>), possibly influencing its digestibility and sensory attributes (<xref ref-type="bibr" rid="ref171">Tomotake et al., 2006</xref>). The CM fat composition is dominated by higher-molecular-weight triacylglycerols (&#x2265;C40 carbons), with low levels of C24&#x2013;C40 and high levels of C48&#x2013;C52, resulting in a higher melting temperature (32.6&#x202F;&#x00B0;C) compared to that of BM (22.8&#x202F;&#x00B0;C) (<xref ref-type="bibr" rid="ref159">Smiddy et al., 2012</xref>). Goat milk (GM) yogurt exhibits higher water-holding capacity than BM yogurt due to its higher protein (3.27% vs. 3.14%) and fat (3.69% vs. 3.33%) contents (<xref ref-type="bibr" rid="ref142">Ragab et al., 2021</xref>). Although understanding the role of fat is essential for developing CM products with desired characteristics, the effects of fat content on the textural and rheological properties of fermented CM remain to be thoroughly investigated.</p>
</sec>
<sec id="sec5">
<label>3.2</label>
<title>Role of starter cultures and fermenting bacteria</title>
<p>CM producers worldwide have developed diverse traditional fermented products, each with its own microbiological, physicochemical, and flavor characteristics (<xref ref-type="table" rid="tab2">Table 2</xref>). These products vary according to fermentation conditions and microbial properties, which are then reflected in the unique sensory characteristics (<xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>; <xref ref-type="bibr" rid="ref154">Shori, 2017</xref>; <xref ref-type="bibr" rid="ref151">Seifu, 2023</xref>). Compared to fermented BM yogurts, the majority of fermented CM products are beverages (i.e., drinkable yogurts) (<xref ref-type="bibr" rid="ref161">Sobti et al., 2021</xref>; <xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>; <xref ref-type="bibr" rid="ref84">Kamal-Eldin et al., 2020</xref>). For example, Chal, a slightly thick beverage popular in Bulgaria, Iran, and Turkey, is fermented by a complicated bacterial consortium mainly consisting of <italic>L. plantarum</italic>, <italic>Lactobacillus kefiri</italic>, and <italic>Enterococcus faecium</italic> (<xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>; <xref ref-type="bibr" rid="ref151">Seifu, 2023</xref>; <xref ref-type="bibr" rid="ref165">Soleymanzadeh et al., 2016</xref>). Doogh, which is consumed in Iran, Afghanistan, and Turkey, is a drinkable yogurt fermented with <italic>Bifidobacterium bifidum</italic> and frequently enriched with salt, ginger extract, pectin, or gum Arabic (<xref ref-type="bibr" rid="ref25">Azarikia and Abbasi, 2010</xref>). Gariss, which is produced by spontaneous fermentation in Sudan, has a liquid to slightly thick consistency (<xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>; <xref ref-type="bibr" rid="ref154">Shori, 2017</xref>). Camel kefir is obtained by spontaneous fermentation of kefir grains under approximately room temperature, resulting in a thick, creamy product that is usually chilled for consumption (<xref ref-type="bibr" rid="ref65">Hamed et al., 2024</xref>; <xref ref-type="bibr" rid="ref154">Shori, 2017</xref>; <xref ref-type="bibr" rid="ref151">Seifu, 2023</xref>). Other traditional fermented CM products include Laban, Shubat, Susuac, and Zrig (<xref ref-type="bibr" rid="ref129">Muthukumaran et al., 2023</xref>; <xref ref-type="bibr" rid="ref151">Seifu, 2023</xref>; <xref ref-type="bibr" rid="ref33">Chammas et al., 2006</xref>).</p>
<table-wrap position="float" id="tab2">
<label>Table 2</label>
<caption>
<p>Different traditionally fermented camel milk products consumed worldwide.</p>
</caption>
<table frame="hsides" rules="groups">
<thead>
<tr>
<th align="left" valign="top">Product name</th>
<th align="left" valign="top">Bacteria used</th>
<th align="left" valign="top">Fermentation &#x0026; storage conditions</th>
<th align="left" valign="top">Additives</th>
<th align="left" valign="top">Texture</th>
<th align="left" valign="top">Reference</th>
</tr>
</thead>
<tbody>
<tr>
<td align="left" valign="top">Chal (Bulgaria, Iran, and Turkey)</td>
<td align="left" valign="top"><italic>L. plantarum, L. paraplantarum, Lb. kefiri, Lb. gasseri, Lacticaseibacillus. paracasei, Leuconostoc lactis, Weissella cibaria,</italic> &#x0026; <italic>Enterococcus (E.) faecium</italic></td>
<td align="left" valign="top">pH 4.3&#x2013;4.6, Temp 22&#x2013;28&#x202F;&#x00B0;C, incubated in earthenware jug, Stored in skin bags</td>
<td align="left" valign="top">None</td>
<td align="left" valign="top">Slightly thick</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref65">Hamed et al. (2024)</xref>, <xref ref-type="bibr" rid="ref151">Seifu (2023)</xref>, and <xref ref-type="bibr" rid="ref165">Soleymanzadeh et al. (2016)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Doogh (Iran, Afghanistan, Turkey)</td>
<td align="left" valign="top"><italic>Bifidobacterium bifidum</italic></td>
<td align="left" valign="top">pH 3.64&#x2013;4.2, Temp 37&#x2013;38&#x202F;&#x00B0;C, Stored at 5&#x2013;7&#x202F;&#x00B0;C,</td>
<td align="left" valign="top">Salt, ginger extract, pectin, gum arabic</td>
<td align="left" valign="top">Thin, drinkable</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref25">Azarikia and Abbasi (2010)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Gariss (Sudan)</td>
<td align="left" valign="top">Spontaneous fermentation</td>
<td align="left" valign="top">pH 3.4&#x2013;3.7, Temp 30&#x2013;37&#x202F;&#x00B0;C, Ambient</td>
<td align="left" valign="top">None</td>
<td align="left" valign="top">Liquid, slightly thick</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref65">Hamed et al. (2024)</xref> and <xref ref-type="bibr" rid="ref154">Shori (2017)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Kefir (Modified Camel Kefir)</td>
<td align="left" valign="top">Spontaneous fermentation</td>
<td align="left" valign="top">pH 4.3&#x2013;4.4, Temp 20&#x2013;26&#x202F;&#x00B0;C, Refrigerated, short-term</td>
<td align="left" valign="top">Kefir grains</td>
<td align="left" valign="top">Thick, slightly creamy</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref65">Hamed et al. (2024)</xref>, <xref ref-type="bibr" rid="ref154">Shori (2017)</xref>, and <xref ref-type="bibr" rid="ref151">Seifu (2023)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Laban (Middle East, North Africa)</td>
<td align="left" valign="top"><italic>S. thermophilus, Lb. bulgaricus</italic></td>
<td align="left" valign="top">pH 3.98&#x2013;4.52, Temp 40&#x2013;45&#x202F;&#x00B0;C, Refrigerated</td>
<td align="left" valign="top">None or salt</td>
<td align="left" valign="top">Semi-liquid, smooth</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref33">Chammas et al. (2006)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Shubat (Kazakhstan)</td>
<td align="left" valign="top">Spontaneous fermentation</td>
<td align="left" valign="top">pH 3.7&#x2013;4.1, Temp 25&#x2013;30&#x202F;&#x00B0;C, Refrigerated or ambient</td>
<td align="left" valign="top">None</td>
<td align="left" valign="top">Liquid, slightly viscous</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref129">Muthukumaran et al. (2023)</xref> and <xref ref-type="bibr" rid="ref65">Hamed et al. (2024)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Suusac (Somalia, Kenya)</td>
<td align="left" valign="top">Spontaneous fermentation</td>
<td align="left" valign="top">pH 3.6&#x2013;4.9, Temp 26&#x2013;29&#x202F;&#x00B0;C, Stored in smoked containers</td>
<td align="left" valign="top">Smoke-treated gourds</td>
<td align="left" valign="top">Thin, slightly foamy</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref65">Hamed et al. (2024)</xref> and <xref ref-type="bibr" rid="ref154">Shori (2017)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Zrig (Mauritania)</td>
<td align="left" valign="top">Spontaneous fermentation</td>
<td align="left" valign="top">pH 4.2&#x2013;4.5, Temp 25&#x2013;30&#x202F;&#x00B0;C, Consumed fresh</td>
<td align="left" valign="top">Sugar millet</td>
<td align="left" valign="top">Thin, drinkable</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref151">Seifu (2023)</xref>
</td>
</tr>
</tbody>
</table>
</table-wrap>
<p><xref ref-type="fig" rid="fig6">Figure 6</xref> illustrates the mutualistic interaction between <italic>Lb. delbrueckii</italic> subsp. <italic>bulgaricus</italic> and <italic>S. thermophilus</italic> in the fermentation of milk. These interactions are crucial for establishing the appropriate microbial ecosystem in milk fermentation, ensuring the quality and safety of the final product (<xref ref-type="bibr" rid="ref181">Yang et al., 2025</xref>). Synergistic interactions between these bacteria involve metabolite exchange, protein and amino acid metabolism, lactic acid and acidity regulation, urea activity, pH regulation, exopolysaccharide production, and glutathione production (<xref ref-type="bibr" rid="ref22">Ayivi and Ibrahim, 2022</xref>). <italic>S. thermophilus</italic> enhances the growth of <italic>Lb. bulgaricus</italic> and metabolism by producing ammonia, formic acid, and folic acid, while <italic>Lb. bulgaricus</italic> hydrolyzes milk proteins into the growth-promoting peptides and amino acids used by <italic>S. thermophilus</italic> (<xref ref-type="bibr" rid="ref181">Yang et al., 2025</xref>). <italic>S. thermophilus</italic> consumes oxygen (O<sub>2</sub>) in the fermentation medium, producing carbon dioxide (CO<sub>2</sub>), which is preferred by <italic>Lb. bulgaricus</italic> (<xref ref-type="bibr" rid="ref150">Sasaki et al., 2014</xref>). Additionally, <italic>Lb. bulgaricus</italic> produces lactic acid, which adds to the acidity of the yogurt, by breaking down casein into peptides and amino acids through the expression of proteases (<xref ref-type="bibr" rid="ref22">Ayivi and Ibrahim, 2022</xref>). <italic>Lb. bulgaricus</italic> and <italic>S. thermophilus</italic> produce long-chain fatty acids and glutathione, which maintain membrane stability and oxidative stress resistance (<xref ref-type="bibr" rid="ref181">Yang et al., 2025</xref>). This proto-cooperation ensures optimal growth, metabolite exchange, and stability in yogurt fermentation (<xref ref-type="bibr" rid="ref22">Ayivi and Ibrahim, 2022</xref>). Bacteria produce several fermentation products such as lactic acid, flavor components, and EPS, enhancing the yogurt&#x2019;s texture and mouthfeel. Their mutual metabolic exchange ensures stability and optimal growth, driving efficient milk fermentation (<xref ref-type="bibr" rid="ref175">Wang J. et al., 2025</xref>). This symbiosis highlights the importance of microbial interactions in achieving stable coexistence and efficient substrate conversion in food fermentation. Therefore, understanding the connection between <italic>Lb. bulgaricus</italic> and <italic>S. thermophilus</italic> may contribute to enhancing the texture, flavor, and quality of fermented dairy products by optimizing strain selection or process conditions.</p>
<fig position="float" id="fig6">
<label>Figure 6</label>
<caption>
<p>Schematic representation of the interactions between <italic>S. thermophilus</italic> and <italic>Lb. bulgaricus</italic> during yogurt fermentation and their effects on product attributes. The dotted lines are related to EPS, which are hypothesized to mediate the exchange of metabolites between the two species in proximity: production or enzymatic activity; positive effect of the component; negative effect; neutral or yet to be proven effect. LCFA: long-chain fatty acid; EPS: exopolysaccharides [adapted from <xref ref-type="bibr" rid="ref181">Yang et al. (2025)</xref> and <xref ref-type="bibr" rid="ref22">Ayivi and Ibrahim (2022)</xref>] under creative commons permission.</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g006.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Diagram showing the metabolic interaction between Streptococcus thermophilus and Lactobacillus bulgaricus in yogurt production. Arrows illustrate the exchange of urea, ammonia, peptides, amino acids, lactic acid, and other compounds, promoting processes like peptidolysis, proteolysis, gel formation, and coagulation. Whey proteins and casein are also involved.</alt-text>
</graphic>
</fig>
<p>As schematically outlined in <xref ref-type="fig" rid="fig7">Figure 7</xref>, bacterial cells quickly sense their surroundings and initiate transcription during the different phases of bacterial growth. A transcriptomic analysis of the lag phase helped to identify the regulatory mechanisms that govern the transitions from the stationary to lag phases and from the lag to exponential phases, where aerobic respiration is fully established and tricarboxylic acid (TCA) cycle enzymes and metal uptake systems support growth (<xref ref-type="bibr" rid="ref146">Rolfe et al., 2012</xref>). The stationary phase is characterized by low TCA cycle components, active Fe&#x2013;S cluster formation, strong expression of genes involved in the stress response systems and protein repair pathways, and anaerobic respiration. Increased protein repair and the production of Fe&#x2013;S clusters occur as a result of the oxidative stress response that is initiated during the lag phase (<xref ref-type="bibr" rid="ref146">Rolfe et al., 2012</xref>). Two exponential growth phases, each distinguished by significant interactions and metabolic alterations, are separated by a transition phase.</p>
<fig position="float" id="fig7">
<label>Figure 7</label>
<caption>
<p><bold>(A)</bold> The major physiological processes occurring during the three phases of bacterial growth (stationary, lag, and exponential). The processes and functional protein groups are depicted according to the varying levels of gene expression in each growth phase: blue, low expression; yellow, medium expression; red, high expression [adapted from <xref ref-type="bibr" rid="ref146">Rolfe et al. (2012)</xref>] with permission from American Society for Microbiology. <bold>(B)</bold> Schematic diagram showing the different bacterial growth phases during milk fermentation. The growth trajectories of <italic>S. thermophilus</italic> and <italic>Lb. bulgaricus</italic> are shown by the green and red curves, respectively. AA: amino acid; EPS: exopolysaccharide; LCFA: long-chain fatty acid [adapted from <xref ref-type="bibr" rid="ref181">Yang et al. (2025)</xref>] under creative commons permission.</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g007.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Diagram illustrating bacterial growth phases (lag, exponential, stationary) with corresponding cellular processes. Panel A shows high expression of RNA polymerase and TCA cycle during exponential growth, with protein repair and overflow metabolism. Panel B depicts cell density changes over time, highlighting key metabolic shifts like glucose utilization, enzyme formation, and growth inhibition by acid in the stationary phase. Two bacterial species are noted: &#x002A;S. thermophilus&#x002A; and &#x002A;Lb. bulgaricus&#x002A;.</alt-text>
</graphic>
</fig>
<p><italic>S. thermophilus</italic> can withstand neutral pH and efficiently uptake amino acids (<xref ref-type="bibr" rid="ref155">Sieuwerts, 2016</xref>), which may promote its faster growth in the lag phase as an adaption to the milk environment. The first exponential phase (<xref ref-type="fig" rid="fig7">Figure 7</xref>) is the most common, which generates carbon dioxide, lactic acid, formic acid, and folic acid. <italic>S. thermophilus</italic> provides folic acid and formic acid, which <italic>Lb. bulgaricus</italic> requires for its growth (<xref ref-type="bibr" rid="ref102">Lecomte et al., 2016</xref>), while the bacterium&#x2019;s consumption of oxygen, and consequent production of carbon dioxide, promotes the anaerobic growth of <italic>Lb. bulgaricus</italic> (<xref ref-type="bibr" rid="ref150">Sasaki et al., 2014</xref>). <italic>S. thermophilus</italic> hydrolyzes lactose by utilizing <italic>&#x03B2;</italic>-galactosidase, resulting in the production of glucose and galactose, which are then glycolyzed to generate lactic acid in milk (<xref ref-type="bibr" rid="ref168">Tarrah et al., 2018</xref>). The limited availability of amino acids slows bacterial growth during the transition phase. <italic>Lb. bulgaricus</italic> activates the <italic>prtB</italic> gene, generating an extracellular protease that breaks down casein into peptides and amino acids, providing nitrogen sources to promote the growth of both bacteria (<xref ref-type="bibr" rid="ref108">Liu et al., 2016</xref>). The second exponential phase during milk fermentation involves the growth of <italic>Lb. bulgaricus</italic> and <italic>S. thermophilus</italic>, which upregulate pathways for the synthesis of long-chain fatty acid and glutathione (<xref ref-type="bibr" rid="ref181">Yang et al., 2025</xref>). These conditions offer advantages to the growth of <italic>Lb. bulgaricus</italic> by raising pH and improving acidification, lactose utilization, and lactic acid production (<xref ref-type="bibr" rid="ref184">Yu et al., 2020</xref>). During the stationary phase, bacterial growth is delayed due to acid accumulation; nevertheless, the metabolic synergy between the two species ensures efficient fermentation (<xref ref-type="bibr" rid="ref181">Yang et al., 2025</xref>). Future research could explore the effect of various probiotic strains on fermentation and their contributions to improving the techno-functional properties of fermented dairy products. <italic>S. thermophilus</italic> plays a major role in lactose utilization, producing lactic acid, which lowers pH and enhances proteolysis, resulting in the liberation of peptides and amino acids with antimicrobial and antioxidant properties (<xref ref-type="bibr" rid="ref49">Elhamid and Elbayoumi, 2017</xref>). <italic>S. thermophilus</italic> also generates EPS by facilitating water-binding capacity and casein network rigidity, resulting in viscosity improvement and reducing syneresis in BM yogurt (<xref ref-type="bibr" rid="ref182">Yang et al., 2014</xref>; <xref ref-type="bibr" rid="ref41">Daba et al., 2021</xref>). Moreover, strains ST-3021 and ST-4845 are EPS-producing strains that enhance the hardness and texture of yogurt, resulting in a creamier yogurt with a superior mouthfeel (<xref ref-type="bibr" rid="ref54">Folkenberg et al., 2006</xref>). The bacterium interacts synergistically with <italic>Lb. bulgaricus,</italic> further highlighting its importance in commercial yogurt production. Thermophilic lactobacilli, particularly <italic>Lb. bulgaricus</italic>, surpass the fermentation performance other bacteria by exhibiting strong proteolytic activities (proteinases and peptidases), which contribute to flavor development and the formation of bioactive peptides with antimicrobial and antioxidant properties (<xref ref-type="bibr" rid="ref93">Kieliszek et al., 2021</xref>). Strain GL03-1 of <italic>Lb. bulgaricus</italic> was reported to substantially improve the viscoelastic properties of buffalo yogurt, exhibiting a three-dimensional mesh-like gel structure (<xref ref-type="bibr" rid="ref182">Yang et al., 2014</xref>). The combination of <italic>Lb. fermentum</italic> and <italic>Lb. bulgaricus</italic> in BM yogurt increased acid generation and adhesiveness, while decreasing the degree of whey separation, offering an effective fat replacer (<xref ref-type="bibr" rid="ref170">Tiwari et al., 2021</xref>).</p>
<p>Some studies have investigated the influence of other lactobacilli on the fermentation time and yogurt quality. For instance, the addition of <italic>Lb. helveticus</italic> H9 as a starter culture in BM yogurt fermentation led to shorter fermentation times and higher levels of volatile compounds (<xref ref-type="bibr" rid="ref187">Zhou et al., 2019</xref>). <italic>Lb. helveticus</italic> is a probiotic bacterium that can be used as a starter culture in fermented CM and exhibits high proteolytic activity, producing bioactive peptides with therapeutic benefits and antibacterial properties (<xref ref-type="bibr" rid="ref35">Chelladhurai et al., 2024</xref>). Notably, selective strains of <italic>Lb. helveticus</italic> are also considered for imparting nutty and anti-bitter flavors and improving the sensory appeal of fermented CM (<xref ref-type="bibr" rid="ref34">Chelladhurai et al., 2023</xref>). <italic>Lb. helveticus</italic>-fermented CM exhibited high levels of auto-aggregation, coaggregation, and adhesion, demonstrating the ability to adhere to intestinal epithelial cells and offer defense against infections (<xref ref-type="bibr" rid="ref111">Mahmoudi et al., 2019</xref>).</p>
<p>Probiotic <italic>Lactobacillus</italic> strains (<italic>L. plantarum</italic>-KX881772, <italic>L. plantarum</italic>-KX881779, <italic>Lb. reuteri</italic>-KX881777) of CM performed better than non-CM strains (<xref ref-type="bibr" rid="ref70">Hati, 2018</xref>). Research on the incorporation of <italic>L. plantarum</italic> in CM fermentation suggests its potential for industrial utilization. <italic>L. plantarum</italic> HUM19, <italic>Lb. fermentum</italic>, and <italic>Lb. rhamnosus</italic> showed high proteolysis and sensory characteristics in both fermented CM and BM (<xref ref-type="bibr" rid="ref125">Moslehishad et al., 2013</xref>). As a probiotic adjunct culture in yogurt production, <italic>L. plantarum</italic> exhibits strong capacity to enhance functional attributes such as flavor and probiotic viability without compromising sensory profiles, making it a suitable and considerable option for the creation of innovative functional dairy products (<xref ref-type="bibr" rid="ref106">Li et al., 2017</xref>). <italic>L. plantarum</italic> exhibited proficiency in suppressing the proliferation of foodborne pathogens in fermented CM (<xref ref-type="bibr" rid="ref106">Li et al., 2017</xref>), rendering it a secure choice as a primary fermentative. <italic>L. plantarum</italic> was also found to enhance secondary proteolysis in CM, releasing peptides and amino acids that act as flavor precursors (<xref ref-type="bibr" rid="ref119">Mishra et al., 2019</xref>). Mixed starters of <italic>L. plantarum</italic> and <italic>S. thermophilus</italic> exhibited enhanced casein breakdown and modified proteolysis patterns (<xref ref-type="bibr" rid="ref107">Li et al., 2019</xref>). Moreover, <italic>L. plantarum</italic> KX041 produces EPS with free radical-scavenging activity during fermentation (<xref ref-type="bibr" rid="ref179">Xu et al., 2019</xref>). These results highlight the significance of adopting a careful approach when selecting probiotic strains for co-cultures in fermented dairy production (<xref ref-type="bibr" rid="ref107">Li et al., 2019</xref>).</p>
<p>According to <xref ref-type="bibr" rid="ref27">Bandiera et al. (2013)</xref>, <italic>Lb. casei</italic> can be effectively incorporated into yogurt without negatively affecting other starter cultures. The probiotic strain <italic>Lb. casei</italic> (<xref ref-type="bibr" rid="ref26">Bai et al., 2020</xref>) shortened the fermentation time and increased beneficial EPS production, resulting in higher bacterial viability, improved viscosity and enhanced gel structures in fermented CM (<xref ref-type="bibr" rid="ref26">Bai et al., 2020</xref>; <xref ref-type="bibr" rid="ref103">Lee and Lucey, 2004</xref>; <xref ref-type="bibr" rid="ref176">Wang D. et al., 2025</xref>). <italic>Lb. casei</italic> and <italic>Lb. acidophilus</italic> enhanced the antioxidant capacity in probiotic BM yogurt by releasing potent peptides with free radical-scavenging and metal-chelating properties (<xref ref-type="bibr" rid="ref53">Fardet and Rock, 2018</xref>; <xref ref-type="bibr" rid="ref167">Tadesse and Emire, 2020</xref>). In commercial products such as Yakult<sup>&#x00AE;</sup> and Actimel<sup>&#x2122;</sup>, fermentation with <italic>Lb. casei</italic> alone generated volatile compounds dominated by acetic acid, acetoin, and butyric acid. When combined with other yogurt cultures, <italic>Lb. casei</italic> increased the levels of 3-hydroxy-2-butanone and hexanoic acid in BM yogurt, thereby enhancing the yogurt-like aroma (<xref ref-type="bibr" rid="ref37">Chen et al., 2017</xref>; <xref ref-type="bibr" rid="ref185">Zar&#x0119;ba et al., 2014</xref>). <xref ref-type="table" rid="tab3">Table 3</xref> summarizes the techno-functional effects of various LAB strains and species on the properties of yogurts and fermented camel milk products.</p>
<table-wrap position="float" id="tab3">
<label>Table 3</label>
<caption>
<p>Techno-functional properties of different milk products fermented with different types of lactic acid bacteria.</p>
</caption>
<table frame="hsides" rules="groups">
<thead>
<tr>
<th align="left" valign="top">Culture</th>
<th align="left" valign="top">Techno-functional effects</th>
<th align="left" valign="top">References</th>
</tr>
</thead>
<tbody>
<tr>
<td align="left" valign="top"><italic>Lb. helveticus</italic> H9</td>
<td align="left" valign="top">Shortens fermentation time, increases volatile components</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref187">Zhou et al. (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lactiplantibacillus plantarum</italic> IMAU80106, IMAU10216, IMAU70095</td>
<td align="left" valign="top">Increases the coagulation ability and proteolytic activity</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref106">Li et al. (2017)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lb. casei Zhang</italic></td>
<td align="left" valign="top">Shortens fermentation time, increases EPS production &#x0026; improves texture</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref26">Bai et al. (2020)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>S. thermophilus</italic> S-3</td>
<td align="left" valign="top">Decreases syneresis</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref180">Xu et al. (2018)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>S. thermophilus</italic> CC30</td>
<td align="left" valign="top">Has emulsification properties</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref86">Kanamarlapudi and Muddada (2017)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>L. plantarum</italic> C70</td>
<td align="left" valign="top">Improves texture &#x0026; rheological properties</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref24">Ayyash et al. (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>S. thermophilus</italic> LY03</td>
<td align="left" valign="top">Increases apparent viscosity</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref44">De Vuyst et al. (2003)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lb. delbrueckii ssp. bulgaricus</italic> DGCC291</td>
<td align="left" valign="top">Increases viscosity &#x0026; decreases syneresis</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref59">Gent&#x00E8;s et al. (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>L. plantarum</italic> YW11</td>
<td align="left" valign="top">Improves viscosity of skim milk yogurt</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref177">Wang et al. (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>S. thermophilus</italic> CH101, NIZO 2104</td>
<td align="left" valign="top">Increases viscosity &#x0026; decreases syneresis</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref59">Gent&#x00E8;s et al. (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lb. casei Zhang</italic></td>
<td align="left" valign="top">Improves viscosity and promotes gel formation</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref176">Wang D. et al. (2025)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>S. thermophilus</italic> CH101</td>
<td align="left" valign="top">Produces exopolysaccharides (EPS)</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref44">De Vuyst et al. (2003)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lb. casei LcS</italic></td>
<td align="left" valign="top">Contributes anti-obesity effects</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref88">Karimi et al. (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>L. plantarum</italic> OLL2712</td>
<td align="left" valign="top">Contributes anti-diabetic effects</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref172">Toshimitsu et al. (2016)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top"><italic>Lb. helveticus</italic> 881315</td>
<td align="left" valign="top">Produces angiotensin-converting enzyme (ACE) inhibitory peptides</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref153">Shi et al. (2016)</xref>
</td>
</tr>
</tbody>
</table>
</table-wrap>
</sec>
<sec id="sec6">
<label>3.3</label>
<title>Effects of processing and fermentation conditions</title>
<p>In addition to the milk type and bacterial strain, the processing conditions such as heat treatment, pressure, homogenization, and additives are key variables that affect yogurt quality. Conventional heat treatments prior to fermentation have detrimental effects on the organoleptic qualities of fermented milk products (i.e., texture, creation of off-flavors, and color) (<xref ref-type="bibr" rid="ref19">Asaduzzaman et al., 2021</xref>; <xref ref-type="bibr" rid="ref183">Yirda et al., 2020</xref>). In addition to deactivating enzymes and extending the shelf life of milk by destroying pathogenic microbes and spoiling either completely or partially (<xref ref-type="bibr" rid="ref71">Hattem et al., 2011</xref>), heat treatment has major effects on the composition of fermented CM and the release of bioactive peptides (<xref ref-type="bibr" rid="ref81">Izadi et al., 2019</xref>). As previously mentioned, the denaturation of milk whey proteins and their bonding with <italic>&#x03BA;</italic>-casein are the most significant consequences of heating milk (<xref ref-type="bibr" rid="ref58">Genene et al., 2018</xref>). &#x03BA;-Casein interacts with sulfhydryl-disulfide bonds during heating above 70&#x202F;&#x00B0;C to produce micelle-bound and soluble thermal co-aggregates (<xref ref-type="bibr" rid="ref19">Asaduzzaman et al., 2021</xref>), which has an impact on the protein network and the gelation characteristics of casein micelles (<xref ref-type="bibr" rid="ref120">Mohamed et al., 2022b</xref>). Compared to BM, CM was reported to be less stable and more susceptible to heat treatments (<xref ref-type="bibr" rid="ref120">Mohamed et al., 2022b</xref>). A typical pasteurization procedure for CM is 60&#x202F;&#x00B0;C for 30&#x202F;min, 63&#x202F;&#x00B0;C for 30&#x202F;min, and 75&#x202F;&#x00B0;C for 15&#x202F;s (<xref ref-type="bibr" rid="ref9">Alhaj et al., 2013</xref>). Thermally treated CM (63&#x202F;&#x00B0;C for 30&#x202F;min, 72&#x202F;&#x00B0;C for 15&#x202F;s, and 100.5&#x202F;&#x00B0;C for 10&#x202F;min) reduced the overall acceptability, taste score, and texture compared to those of untreated milk (<xref ref-type="bibr" rid="ref109">Lund et al., 2019</xref>). Moreover, CM exhibited poor heat stability when autoclaved for 15&#x202F;min at 121&#x202F;&#x00B0;C, resulting in sedimentation and whey separation (<xref ref-type="bibr" rid="ref9">Alhaj et al., 2013</xref>). Prior heating of the milk for 10&#x2013;15&#x202F;min at 80&#x202F;&#x00B0;C&#x2013;95&#x202F;&#x00B0;C promotes protein network development, water retaining capabilities, enzyme denaturation, and the destruction of unavoidable microbes. Whey separation and textural flaws may be reduced by optimizing the incubation temperature (&#x223C;40&#x202F;&#x00B0;C), which can eventually improve the yogurt texture (<xref ref-type="bibr" rid="ref103">Lee and Lucey, 2004</xref>).</p>
<p><xref ref-type="table" rid="tab4">Table 4</xref> shows the effects of various fermentation pre-treatments, including thermal processing, homogenization, HPP, fermentation, and thermosonication (<xref ref-type="bibr" rid="ref90">Kenari and Razavi, 2021</xref>). By adopting non-thermal technology, most of the adverse effects of thermal treatment can be avoided, leading to higher-quality food products (<xref ref-type="bibr" rid="ref4">Ahmad et al., 2019</xref>). Milk homogenization was reported to improve BM yogurt quality by reducing the size of fat globules (<xref ref-type="bibr" rid="ref74">Ho et al., 2022b</xref>; <xref ref-type="bibr" rid="ref173">Trujillo et al., 2016</xref>). However, since CM is naturally characterized by smaller and more homogeneous fat globules than BM, it does not require homogenization (<xref ref-type="table" rid="tab1">Table 1</xref>). HPP can enhance the rheological characteristics of fermented BM by modifying milk proteins, such as whey protein denaturation and casein micelle disruption due to colloidal calcium phosphate solubilization (<xref ref-type="bibr" rid="ref130">Nassar et al., 2020</xref>). HPP treatment at 300 and 600&#x202F;mPa for 10&#x202F;min at 10&#x202F;&#x00B0;C could maintain the greatest bacterial counts. While high-temperature short-time and UHT treatments increase the particle size in BM, the opposite effect is found in CM (<xref ref-type="bibr" rid="ref23">Ayyash et al., 2022</xref>). HPP treatment lowered the particle size in both CM and BM and produced yogurts with creamier mouthfeels and smoother textures (<xref ref-type="bibr" rid="ref23">Ayyash et al., 2022</xref>). Furthermore, fermented heat-treated CM produced stronger gels with better storage properties and less modulus loss than HPP-treated milk, notably with treatment at 85&#x202F;&#x00B0;C, whereas ultrafiltration increased only the viscosity and not the gel strength (<xref ref-type="bibr" rid="ref162">Sobti et al., 2024</xref>). Therefore, HPP is inferior to heat treatment in enhancing fermented CM texture. Thus, the observed difference can be attributed to the differences between CM and BM in the original micelle structure and how these are affected by heating and HPP treatments.</p>
<table-wrap position="float" id="tab4">
<label>Table 4</label>
<caption>
<p>The effect of pre-fermentation conditions on the quality of fermented camel milk (CM) products.</p>
</caption>
<table frame="hsides" rules="groups">
<thead>
<tr>
<th align="left" valign="top">Treatment</th>
<th align="left" valign="top">Key findings</th>
<th align="left" valign="top">References</th>
</tr>
</thead>
<tbody>
<tr>
<td align="left" valign="top">Prior heating (85&#x202F;&#x00B0;C, 30&#x202F;min)</td>
<td align="left" valign="top">Heat-treatment enhanced the texture and rheological properties signifying stronger gels.</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref162">Sobti et al. (2024)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Ultra-high temperature (UHT-140&#x202F;&#x00B0;C, 3&#x202F;s)</td>
<td align="left" valign="top">UHT &#x0026; HPP increased the viscosity and HPP improved the rheological properties (G&#x2032; and G&#x2032;&#x2032;)</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref23">Ayyash et al. (2022)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">High-Pressure Processing (HPP) (350/550&#x202F;MPa, 5&#x202F;min)</td>
<td align="left" valign="top">HPP-treated fermented CM had lower viscosity than heat-treated milk</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref23">Ayyash et al. (2022)</xref> and <xref ref-type="bibr" rid="ref162">Sobti et al. (2024)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Fermentation temperature (40&#x202F;&#x00B0;C, pH 4.6)</td>
<td align="left" valign="top">Lower incubation temperatures increased storage modulus &#x0026; yield stress and reduced whey separation &#x0026; textural defects</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref103">Lee and Lucey (2004)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Thermosonication (75% amplitude, 55&#x202F;&#x00B0;C, 10&#x202F;min)</td>
<td align="left" valign="top">Reduced syneresis and improved acidity, texture, flavor, &#x0026; color</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref90">Kenari and Razavi (2021)</xref>
</td>
</tr>
</tbody>
</table>
</table-wrap>
<p>The combination of low incubation temperatures and moderate to high inoculation rates can enhance the gel strength and storage modulus, thereby enhancing the texture of BM yogurt (<xref ref-type="bibr" rid="ref103">Lee and Lucey, 2004</xref>). In the dairy sector, the application of ultrasound has been used to regulate the functional qualities of dietary proteins as well as the microstructure and texture of fat-containing items, including yogurt, cheese, and ice cream (<xref ref-type="bibr" rid="ref4">Ahmad et al., 2019</xref>). Moreover, ultrasound inactivates microorganisms and enzymes (<xref ref-type="bibr" rid="ref4">Ahmad et al., 2019</xref>), develops a sweetening effect in yogurt (<xref ref-type="bibr" rid="ref178">Wu et al., 2000</xref>), enhances emulsification and homogenization by decreasing the size of milk fat globules, and shortens fermentation times by enhancing lactose hydrolysis in yogurt production (<xref ref-type="bibr" rid="ref8">Akdeniz and Akal&#x0131;n, 2019</xref>). High-intensity ultrasound treatment was reported to improve various characteristics of BM, including the denaturation of casein micelles, formation of aggregates between <italic>&#x03BA;</italic>-casein and whey proteins (<italic>&#x03B2;</italic>-lactoglobulin), viscosity, texture, fat globule size, and surface membrane area (<xref ref-type="bibr" rid="ref8">Akdeniz and Akal&#x0131;n, 2019</xref>).</p>
<p>Thermosonication considerably improved the qualities of fermented CM, providing a potentially viable method for improving yogurt quality. The ideal parameters for thermosonication of CM are 55&#x202F;&#x00B0;C for 10&#x202F;min at 75 amplitudes (<xref ref-type="bibr" rid="ref90">Kenari and Razavi, 2021</xref>). The texture of set and stirred yogurt was also influenced by sonication during BM fermentation, which may result in improved smoothness and creaminess (<xref ref-type="bibr" rid="ref96">K&#x00F6;rzend&#x00F6;rfer et al., 2017</xref>). By comprehensively understanding the impacts of manufacturing processes on the final product, the processes may be optimized to produce fermented CM with desired textural features. <xref ref-type="fig" rid="fig8">Figure 8</xref> presents a summary overview of processing and fermentation conditions that enhance, have limited influence on, degrades the quality of fermented CM.</p>
<fig position="float" id="fig8">
<label>Figure 8</label>
<caption>
<p>A schematic overview of processing and fermentation condition that enhance, have limited influence on, and degrade the texture of fermented camel milk.</p>
</caption>
<graphic xlink:href="fmicb-17-1752671-g008.tif" mimetype="image" mime-subtype="tiff">
<alt-text content-type="machine-generated">Chart comparing processes affecting texture. Enhanced texture methods: pre-fermentation heating at eighty degrees Celsius for fifteen minutes or ninety-five degrees Celsius for five minutes, appropriate culture selection, fermentation optimization. Limited or inconsistent effects: homogenization, high-pressure processing. Degrades texture: excessive thermal load, autoclaving, ultra-high temperature processing.</alt-text>
</graphic>
</fig>
</sec>
<sec id="sec7">
<label>3.4</label>
<title>Effect of additives, coagulants, and texture enhancers</title>
<p><xref ref-type="table" rid="tab5">Table 5</xref> summarizes the effects of coagulants and texture-enhancing additives on the quality of fermented products: these additives result in more calcium, phosphorus, and saturated fatty acids in fermented CM, whereas the protein, lactose, and total solids are enhanced in BM yogurt, contributing to its preferred flavor and texture (<xref ref-type="bibr" rid="ref55">Galeboe et al., 2018</xref>). Fortifying CM with milk from other species such as sheep, buffalo, and bovine has been proposed as a potential strategy to enhance the texture and minimize syneresis (<xref ref-type="bibr" rid="ref84">Kamal-Eldin et al., 2020</xref>; <xref ref-type="bibr" rid="ref6">Ait El Alia et al., 2023</xref>; <xref ref-type="bibr" rid="ref77">Ibrahem and El Zubeir, 2016</xref>). Compared to the yogurt produced entirely with CM, yogurt manufactured using a combination of CM and BM had better physicochemical properties and sensory profile (<xref ref-type="bibr" rid="ref84">Kamal-Eldin et al., 2020</xref>; <xref ref-type="bibr" rid="ref128">Mustafa, 2015</xref>). Sheep milk (40&#x2013;60%) (<xref ref-type="bibr" rid="ref77">Ibrahem and El Zubeir, 2016</xref>) and buffalo milk (90%) (<xref ref-type="bibr" rid="ref92">Khalifa and Zakaria, 2018</xref>) increased the total solids content and acceptability of fermented CM, while oat milk (40%) improved the antioxidants, viscosity, and sensory qualities (<xref ref-type="bibr" rid="ref21">Atwaa et al., 2020</xref>). The enhancement of fermented CM quality by the fortification with milks from other animals was attributed to the differences in composition of third portions, especially the contents of <italic>&#x03B2;</italic>-lactoglobulin and <italic>&#x03BA;</italic>-casein. Fortification of CM with BM powder improved the hardness and consistency of fermented CM gels and minimize syneresis during the processing and storage phases (<xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin, 2019</xref>; <xref ref-type="bibr" rid="ref21">Atwaa et al., 2020</xref>; <xref ref-type="bibr" rid="ref149">Salih and Hamid, 2013</xref>; <xref ref-type="bibr" rid="ref134">Omar et al., 2019</xref>). Acid gelation of fermented CM was shown be aided by sodium caseinate prepared from CM casein micelles, which lead to improved texture and rheological properties of the gel (<xref ref-type="bibr" rid="ref175">Wang J. et al., 2025</xref>), suggesting that casein source and structural compatibility are significant factors for effective coagulation. Supplementation with high levels of casein or whey protein was shown to increase syneresis by creating larger porous and less linked aggregates (<xref ref-type="bibr" rid="ref141">Puvanenthiran et al., 2002</xref>) suggesting the need for optimized levels of added milk proteins.</p>
<table-wrap position="float" id="tab5">
<label>Table 5</label>
<caption>
<p>The effect of texture-enhancing additives on fermented camel milk (CM).</p>
</caption>
<table frame="hsides" rules="groups">
<thead>
<tr>
<th align="left" valign="top">Additive</th>
<th align="left" valign="top">Rheology</th>
<th align="left" valign="top">Syneresis</th>
<th align="left" valign="top">Sensory acceptability</th>
<th align="left" valign="top">Mechanism</th>
<th align="left" valign="top">References</th>
</tr>
</thead>
<tbody>
<tr>
<td align="left" valign="top">Bovine milk &#x0026; powder</td>
<td align="left" valign="top">Gel strength, firmness &#x0026; viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Provides &#x03B2;-lactoglobulin and &#x03BA;-casein enhancing protein network, increased total solids</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref84">Kamal-Eldin et al. (2020)</xref> and <xref ref-type="bibr" rid="ref128">Mustafa (2015)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Buffalo milk (90%)</td>
<td align="left" valign="top">Firmness &#x0026; viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">High protein and fat improve network density</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref92">Khalifa and Zakaria (2018)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Sheep milk (40&#x2013;60%)</td>
<td align="left" valign="top">Firmness &#x0026; viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Increased total solids, proteins &#x0026; fat strengthen gel</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref77">Ibrahem and El Zubeir (2016)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Oat milk (40%)</td>
<td align="left" valign="top">Viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Increased phenolic content, antioxidants, and dietary fiber contents</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref21">Atwaa et al. (2020)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">BM casein (2.5%) &#x0026; whey protein (4%)</td>
<td align="left" valign="top">Gel strength, firmness &#x0026; viscosity improved</td>
<td align="left" valign="top">Reduced up to optimal level</td>
<td align="left" valign="top">Reduced up to optimal level</td>
<td align="left" valign="top">Additional milk proteins enhance protein&#x2013;protein interactions and network continuity</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref163">Sobti and Kamal-Eldin (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Sodium caseinate (2.5%)</td>
<td align="left" valign="top">Firmness and water holding capacity increased</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Caseinate improves acid-induced gelation by reinforcing casein network</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref175">Wang J. et al. (2025)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Pea protein (3&#x2013;6%)</td>
<td align="left" valign="top">Gelation and viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Plant proteins reinforce protein&#x2013;protein interactions</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref133">Olaimat et al. (2023)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Gelatin (0.75&#x2013;1.0%)</td>
<td align="left" valign="top">Hardness and viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">-</td>
<td align="left" valign="top">Thermoreversible gel traps water in matrix</td>
<td align="left" valign="top"><xref ref-type="bibr" rid="ref73">Ho et al. (2022a)</xref> and <xref ref-type="bibr" rid="ref126">Mudgil et al. (2018)</xref></td>
</tr>
<tr>
<td align="left" valign="top">Sodium alginate (0.3 and 0.5%)</td>
<td align="left" valign="top">Viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Ionic gelation and water entrapment, interaction with protein network</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref161">Sobti et al. (2021)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Sodium alginate (0.75%) and CaCl&#x2082; (0.075%)</td>
<td align="left" valign="top">Firmness improved</td>
<td align="left" valign="top">Increased</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Increased ionic calcium from CaCl&#x2082; promoted excessive protein aggregation, resulting in coarse gels and increased syneresis</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref68">Hashim et al. (2009)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Gum arabic (1&#x2013;2%)</td>
<td align="left" valign="top">Texture and viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Hydrocolloid increases water-binding and stabilizes protein matrix</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref82">Jasim et al. (2018)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Xanthan gum (0.75%)</td>
<td align="left" valign="top">Texture, viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Thickening via polysaccharide-water interactions</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref124">Mohsin et al. (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Oat &#x03B2;-glucan (2%)</td>
<td align="left" valign="top">Viscosity, water holding capacity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">&#x03B2;-glucan enhances water-holding capacity and serum viscosity</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref98">Ladjevardi et al. (2016)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Modified starch (3%)</td>
<td align="left" valign="top">Viscosity increased</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Starch granules bind free water and reinforce gel structure</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref78">Ibrahim and Khalifa (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Modified starch (2.5%) and CaCl2 (0.075%)</td>
<td align="left" valign="top">Viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">-</td>
<td align="left" valign="top">CaCl2 increased viscosity but also syneresis, stabilized by starch. Modified starch &#x003E; corn starch.</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref136">Oselu et al. (2022b)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Sweet Potato Powder (3%)</td>
<td align="left" valign="top">Viscosity slightly increased</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Dietary fibers enhance water retention and gel stability</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref134">Omar et al. (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Monk fruit sweetener (0.42&#x2013;2.54%)</td>
<td align="left" valign="top">Viscosity improved</td>
<td align="left" valign="top">-</td>
<td align="left" valign="top">Altered color and sweetness</td>
<td align="left" valign="top">Sweetener modifies serum phase and total solids</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref31">Buchilina and Aryana (2021)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Carob fiber (2%),</td>
<td align="left" valign="top">Cohesiveness improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Dietary fiber strengthens matrix and improves water binding</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref83">Jrad et al. (2021)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Date and orange fibers (4.5%)</td>
<td align="left" valign="top">Texture, viscosity increased</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Orange fiber improved flavor and appearance</td>
<td align="left" valign="top">Orange fibers increase total solids and stabilize gel network than date fibers</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref78">Ibrahim and Khalifa (2015)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Persimmon pulp (5%)</td>
<td align="left" valign="top">Gel strength improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Pulp polysaccharides promote gel formation and shorten fermentation time</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref10">Alia et al. (2023)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Whey protein isolate (WPI-3%)&#x202F;+&#x202F;&#x03BA;-carrageenan (0.1%)&#x202F;+&#x202F;traditional samphire molasses (TSM-3%)&#x202F;+&#x202F;xanthan gum (0.5%)</td>
<td align="left" valign="top">Significantly viscosity increased</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Synergistic protein&#x2013;polysaccharide interactions strengthen gel matrix</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref89">Kavas (2016)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Microbial Transglutaminase (MTGase, 0.4%)</td>
<td align="left" valign="top">Viscosity and gel density improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">-</td>
<td align="left" valign="top">Covalent cross-linking of milk proteins strengthens gel network</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref3">Abou-Soliman et al. (2017)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">MTGase &#x0026; WPC (6.2%)</td>
<td align="left" valign="top">Gel structure improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Combined cross-linking and protein enrichment enhance matrix strength</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref32">Bulca et al. (2022)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Transglutaminase enzyme, glutathione, &#x0026; gelatin (0.5&#x2013;1.0&#x202F;g/300&#x202F;mL)</td>
<td align="left" valign="top">Moderate increase in firmness</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved slightly</td>
<td align="left" valign="top">Enzymatic cross-linking with auxiliary stabilizers improves water retention</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref18">Arslan Amin et al. (2023)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Trisodium citrate (30&#x202F;mmol/L)&#x202F;+&#x202F;MTGase</td>
<td align="left" valign="top">Texture improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Neutral</td>
<td align="left" valign="top">Citrate dissociates micelles, improving MTGase accessibility</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref36">Chen et al. (2019)</xref>
</td>
</tr>
<tr>
<td align="left" valign="top">Fruit purees (15, 25, 25% apricot, blueberry, mango, peach, pineapple, and strawberry)</td>
<td align="left" valign="top">Gel structures, viscosity improved</td>
<td align="left" valign="top">Reduced</td>
<td align="left" valign="top">Improved</td>
<td align="left" valign="top">Fruit solids and fibers enhance gel structure and viscosity</td>
<td align="left" valign="top">
<xref ref-type="bibr" rid="ref160">Sobti et al. (2023)</xref>
</td>
</tr>
</tbody>
</table>
</table-wrap>
<p>Efforts have been made to improve fermented CM quality by adding hydrocolloids such as gelatin, sodium alginate, gum Arabic, and xanthan gum (<xref ref-type="table" rid="tab5">Table 5</xref>). Gelatin (0.75&#x2013;1.0%) (<xref ref-type="bibr" rid="ref126">Mudgil et al., 2018</xref>), and xanthan gum (0.75%) (<xref ref-type="bibr" rid="ref124">Mohsin et al., 2019</xref>), oat &#x03B2;-glucan (2%) (<xref ref-type="bibr" rid="ref98">Ladjevardi et al., 2016</xref>), modified starch (3%) (<xref ref-type="bibr" rid="ref78">Ibrahim and Khalifa, 2015</xref>) improved hardness, viscosity, water holding capacity, and sensory perception and sweet potato powder (3%) reduced syneresis and extended shelf-life (<xref ref-type="bibr" rid="ref134">Omar et al., 2019</xref>). Adding hydrocolloids (gelatin, alginate, gum Arabic, and pectin) to CM containing casein, whey protein, and calcium chloride produced different effects. While alginate and pectin improved texture and rheology and reduced syneresis, gum Arabic and gelatin had small negative effect on hardness and rheology (<xref ref-type="bibr" rid="ref164">Sobti et al., 2020</xref>). When mixed with hydrocolloids (gelatin, gum Arabic, pectin, and sodium alginate), calcium chloride (CaCl&#x2082;) was shown to cause excessive protein aggregation in fermented CM leading to coarse gels, enhanced syneresis, and unwanted stiffness, which reduced consumer acceptance (<xref ref-type="bibr" rid="ref164">Sobti et al., 2020</xref>; <xref ref-type="bibr" rid="ref136">Oselu et al., 2022b</xref>; <xref ref-type="bibr" rid="ref143">Ramasubramanian et al., 2008</xref>). Fat substitutes such as gelatin, k-carrageenan, pectin, inulin, fibers, and starch increased the viscosity, decreased syneresis, and improved overall sensory qualities (<xref ref-type="bibr" rid="ref148">Saleh et al., 2018</xref>; <xref ref-type="bibr" rid="ref21">Atwaa et al., 2020</xref>). Some ingredients were effective primarily in combination, such as whey protein isolate (3%) with <italic>&#x03BA;</italic>-carrageenan (0.1%), samphire molasses (3%), and xanthan gum (0.5%) improved rheological properties (<xref ref-type="bibr" rid="ref89">Kavas, 2016</xref>).</p>
<p>Enzymatic modifications are also being tested to improve the quality and properties of fermented CM products. For example, microbial transglutaminase (MTGase, EC 2.3.2.13), a natural alternative to gelatin for yogurt stabilization, proved to be more effective than the dairy powder components (<xref ref-type="bibr" rid="ref3">Abou-Soliman et al., 2017</xref>). MTGase was shown to enhance the structural, textural, and sensory qualities of fermented CM by improving the microstructure and volatile compounds content (<xref ref-type="bibr" rid="ref32">Bulca et al., 2022</xref>; <xref ref-type="bibr" rid="ref36">Chen et al., 2019</xref>; <xref ref-type="bibr" rid="ref75">Hovjecki et al., 2021</xref>). MTGase is commonly added to fermented dairy products at below 1% concentration (<xref ref-type="bibr" rid="ref18">Arslan Amin et al., 2023</xref>) to strengthen the gel matrix by generating cross links between lysine and glutamate residues of proteins (<xref ref-type="bibr" rid="ref60">Gharibzahedi and Chronakis, 2018</xref>). However, MTGase alone cannot fully improve the poor texture of fermented CM, necessitating milk protein enrichment (<xref ref-type="bibr" rid="ref3">Abou-Soliman et al., 2017</xref>; <xref ref-type="bibr" rid="ref110">Ma et al., 2019</xref>; <xref ref-type="bibr" rid="ref118">Metwalli et al., 2023</xref>; <xref ref-type="bibr" rid="ref66">Han et al., 2020</xref>). Further research is needed to optimize the texture of fermented MTGase-treated CM and testing its interaction with milk proteins and hydrocolloids.</p>
<p>Fruit-based ingredients remain popular among consumers because of added color, flavor, taste, and texture (<xref ref-type="bibr" rid="ref10">Alia et al., 2023</xref>; <xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>; <xref ref-type="bibr" rid="ref143">Ramasubramanian et al., 2008</xref>; <xref ref-type="bibr" rid="ref89">Kavas, 2016</xref>). Flavored CM labans supplemented with fruit purees (25% apricot, blueberry, mango, peach, pineapple, and strawberry) showed higher storage moduli, loss moduli, and viscosity values; enhanced gel structures; and improved acceptable sensory properties (<xref ref-type="bibr" rid="ref160">Sobti et al., 2023</xref>). Monk fruit sweetener (0.42&#x2013;2.54%) can be used in fermented CM to change its color and viscosity, while providing a calorie-free, healthy alternative to traditional sweeteners (<xref ref-type="bibr" rid="ref31">Buchilina and Aryana, 2021</xref>). Plant-based additives including pea protein (3&#x2013;6%) resulted in enhancement of yogurt texture and antioxidant qualities (<xref ref-type="bibr" rid="ref133">Olaimat et al., 2023</xref>), while carob fiber (2%) improved cohesion and water-holding capacity (<xref ref-type="bibr" rid="ref83">Jrad et al., 2021</xref>). Date and orange dietary fiber (4.5%) also improved the texture and probiotic development (<xref ref-type="bibr" rid="ref78">Ibrahim and Khalifa, 2015</xref>) and persimmon pulp (5%) promoted gel formation (<xref ref-type="bibr" rid="ref10">Alia et al., 2023</xref>).</p>
</sec>
</sec>
<sec sec-type="conclusions" id="sec8">
<label>4</label>
<title>Conclusion</title>
<p>Fermented camel milk has been shown to have several health benefits including anti-diabetic, anti-hypercholesterolemic, anti-oxidative activity. Unlike BM, the fermentation of CM does not afford a set yogurt but rather a liquid-like that is better described as &#x201C;drinkable yogurt.&#x201D; Although it is accepted that the absence of <italic>&#x03B2;</italic>-lactoglobulin and the low level of <italic>&#x03BA;</italic>-casein are major contributors to the weak gels in fermented CM products, other components of CM such as the high contents of &#x03B2;-casein and proteolytic products may contribute to this difference. The mechanisms of the interactions between these biochemical constituents and how they collectively limit protein interactions, micellar crosslinking, and network formation during acid gelation are not yet understood. The contribution of mineral equilibria, casein phosphorylation, &#x03B2;-casein hydrophobicity, and proteolysis kinetics in the production of CM gels still remain to be explored. Efforts are still needed for the optimization of protein composition, pre-fermentation heat treatment, selection of appropriate bacterial cultures and fermentation conditions, and additives in order to improve appearance, texture, and viscosity. In the future, it is more practical to concentrate product development efforts on improving premium drinkable or semi-liquid fermented CM products rather than adapting to traditional BM set yogurts. The fermented CM flavor can be enhanced by adding fruit purees, and certain herbs and spices.</p>
</sec>
</body>
<back>
<sec sec-type="author-contributions" id="sec9">
<title>Author contributions</title>
<p>SA: Resources, Writing &#x2013; original draft. MA: Writing &#x2013; review &#x0026; editing. AK-E: Project administration, Conceptualization, Supervision, Funding acquisition, Writing &#x2013; review &#x0026; editing.</p>
</sec>
<ack>
<title>Acknowledgments</title>
<p>The authors sincerely thank the reviewers for their valuable comments on the original manuscript.</p>
</ack>
<sec sec-type="COI-statement" id="sec10">
<title>Conflict of interest</title>
<p>The author(s) declared that this work was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.</p>
<p>MA declared that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision.</p>
</sec>
<sec sec-type="ai-statement" id="sec11">
<title>Generative AI statement</title>
<p>The author(s) declared that Generative AI was not used in the creation of this manuscript.</p>
<p>Any alternative text (alt text) provided alongside figures in this article has been generated by Frontiers with the support of artificial intelligence and reasonable efforts have been made to ensure accuracy, including review by the authors wherever possible. If you identify any issues, please contact us.</p>
</sec>
<sec sec-type="disclaimer" id="sec12">
<title>Publisher&#x2019;s note</title>
<p>All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article, or claim that may be made by its manufacturer, is not guaranteed or endorsed by the publisher.</p>
</sec>
<sec sec-type="supplementary-material" id="sec13">
<title>Supplementary material</title>
<p>The Supplementary material for this article can be found online at: <ext-link xlink:href="https://www.frontiersin.org/articles/10.3389/fmicb.2026.1752671/full#supplementary-material" ext-link-type="uri">https://www.frontiersin.org/articles/10.3389/fmicb.2026.1752671/full#supplementary-material</ext-link></p>
<supplementary-material xlink:href="Image_1.jpeg" id="SM1" mimetype="image/jpeg" xmlns:xlink="http://www.w3.org/1999/xlink"/>
</sec>
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</ref-list>
<fn-group>
<fn fn-type="custom" custom-type="edited-by" id="fn0001">
<p>Edited by: <ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/34672/overview">Vasco Ariston De Carvalho Azevedo</ext-link>, Federal University of Minas Gerais, Brazil</p>
</fn>
<fn fn-type="custom" custom-type="reviewed-by" id="fn0002">
<p>Reviewed by: <ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/1328006/overview">Mohammad Altamimi</ext-link>, An-Najah National University, Palestine</p>
<p><ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/2914110/overview">Sally Sakr</ext-link>, Cairo University, Egypt</p>
</fn>
</fn-group>
<fn-group>
<fn fn-type="abbr" id="abbrev1">
<label>Abbreviations:</label>
<p>BM, Bovine milk; CM, Camel milk; GM, Goat milk; LAB, Lactic acid bacteria; TCA, Tricarboxylic acid; UHT, Ultra-high temperature; WP, Whey protein.</p>
</fn>
</fn-group>
</back>
</article>