Casein chemistry—structure, functions, and applications

Edward P. C. Lai , Apollinaire Tsopmo

Exploration of Foods and Foodomics ›› 2025, Vol. 3 ›› Issue (1) : 101099

PDF (1442KB)
Exploration of Foods and Foodomics ›› 2025, Vol. 3 ›› Issue (1) :101099 DOI: 10.37349/eff.2025.101099
Open Access Review
research-article
Casein chemistry—structure, functions, and applications
Author information +
History +
PDF (1442KB)

Abstract

The health benefits of milk have been acknowledged throughout human history, with scientific research over the past 50 years elucidating its nutritional composition and functional benefits. This article presents a contemporary analysis of modern casein chemistry, emphasizing the specialized engineering of dairy proteins for optimizing resource utilization. It explores the unique structure of casein micelles as supramolecular complexes, where ionic interactions promote electron sharing between phosphoserines and calcium phosphate nanoclusters. This review aims to synthesize recent literature on casein nanocomplexes and explore their potential in industrial applications such as drug delivery and sustainable food engineering. Casein-based bio-nanocomposites have emerged as a significant research interest in food science, offering considerable potential for a wide array of scientific applications, such as drug formulation and nutraceutical delivery. It is crucial for scientists to engage in ongoing research and development efforts to encourage sustainable progress, enhance commercial viability, improve manufacturing processes, and expand the engineering applications of casein micelles toward fostering an eco-friendly industry.

Keywords

casein / curdling / edible coating / hydrogel / hydrolysis / micelles / nanocomposites / proteins

Cite this article

Download citation ▾
Edward P. C. Lai, Apollinaire Tsopmo. Casein chemistry—structure, functions, and applications. Exploration of Foods and Foodomics, 2025, 3 (1) : 101099 DOI:10.37349/eff.2025.101099

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

Aguilera JM, Lillford PJ, editors. Food Materials Science: Principles and Practice. New York, NY: Springer; 2008.

[2]

Helmenstine AM. Why Milk Is White: The Science Behind Milkʼs Color. ThoughtCo. 2024.

[3]

Runthala A, Mbye M, Ayyash M, Xu Y, Kamal—Eldin A. Caseins: Versatility of Their Micellar Organization in Relation to the Functional and Nutritional Properties of Milk. Molecules. 2023; 28: 2023.

[4]

Zhang M, Deng Z, Song H, Zhao C, Zou Y, Li Y, et al. Whey protein and endogenous oligopeptide profiles: A comparative study of human and major domestic animal milk. Food Biosci. 2025; 66: 106309.

[5]

Farhat LB, Selmi H, Toth V, Hoarau A, Suli A, Labas KS, et al. A2 Milk: The Impact of Genetic Variation in Milk Protein on Human Health. Curr Protein Pept Sci. 2025; 26: 751—60.

[6]

Kelly LM, OʼMahony JA, Tobin JT. Genetic variation in bovine milk proteins: Implications for functional and nutritional properties. Int J Dairy Technol. 2025; 78: e13152.

[7]

Szyller H, Antosz K, Batko J, Mytych A, Dziedziak M, Wrześniewska M, et al. Bioactive Components of Human Milk and Their Impact on Childʼs Health and Development, Literature Review. Nutrients. 2024; 16: 1487.

[8]

Maryniak NZ, Sancho AI, Hansen EB, Bøgh KL. Alternatives to Cowʼs Milk—Based Infant Formulas in the Prevention and Management of Cowʼs Milk Allergy. Foods. 2022; 11: 926.

[9]

Røisgård S, Nopp A, Lindam A; SWITCH study group; Nilsson CA, West CE. Basophil allergen threshold sensitivity to casein (casein—specific CD—sens) predicts allergic reactions at a milk challenge in most but not all patients. Immun Inflamm Dis. 2024; 12: e1265.

[10]

Vojdani A, Turnpaugh C, Vojdani E. Immune reactivity against a variety of mammalian milks and plant—based milk substitutes. J Dairy Res. 2018; 85: 358-65.

[11]

Soliman N, Soliman A, Alyafei F, ElSiddig S, Alaaraj N, Hamed N, et al. The varied effects of protein intake during infancy, childhood, and adolescence: Associations with growth metrics, body composition, and pubertal development timelines. World J Adv Res Rev. 2024; 21: 657—66.

[12]

Borer KT. Relevance of Milk Composition to Human Longitudinal Growth from Infancy Through Puberty: Facts and Controversies. Nutrients. 2025; 17: 827.

[13]

Sharma P. ADSA Foundation Scholar Award: Materials science approach to the study of mechanical and diffusion properties in cheese . J Dairy Sci. 2022; 105: 4711-21.

[14]

Yuan Y, Chen C, Guo X, Li B, He N, Wang S. Noncovalent interactions between biomolecules facilitated their application in food emulsionsʼ construction: A review. Compr Rev Food Sci Food Saf. 2024; 23: e13285.

[15]

Banaszewska A, Cruijssen F, van der Vorst JG, Claassen GDH, Kampman JL. A comprehensive dairy valorization model. J Dairy Sci. 2013; 96: 761-79.

[16]

Rebouillat S, Ortega—Requena S. Potential Applications of Milk Fractions and Valorization of Dairy By—Products: A Review of the State—of—the—Art Available Data, Outlining the Innovation Potential from a Bigger Data Standpoint. J Biomater Nanobiotechnol. 2015; 6: 176-203.

[17]

Milk Valorisation Calculator[Internet]. Vesper; c2025 [cited 2025 Jun 1]. Available from: https://vespertool.com/calculators/dairy/milk—valorisation/

[18]

Alalam S, Chamberland J, Gravel A, Perreault V, Britten M, Pouliot Y, et al. Valorization of Concentrated Dairy White Wastewater by Reverse Osmosis in Model Cheese Production. Dairy. 2022; 3: 248-61.

[19]

Buchanan D, Martindale W, Romeih E, Hebishy E. Recent advances in whey processing and valorisation: Technological and environmental perspectives. Int J Dairy Technol. 2023; 76: 291-312.

[20]

Gupta R, Kaur G. Characteristics of casein: The milk protein. AIP Conf Proc. 2023; 2535: 030023.

[21]

Biodegradable Casein—Usage in 3D printing[Internet]. Prezi Inc.; c2025 [cited 2025 Jul 4]. Available from: https://prezi.com/9f4kaceejx08/biodegradable—casein—usage—in—3d—printing/

[22]

Jefferson MT, Rutter C, Fraine K, Borges GVB, de Souza Santos GM, Schoene FAP, et al. Valorization of Sour Milk to Form Bioplastics: Friend or Foe? J Chem Educ. 2020; 97: 1073-6.

[23]

Basnur J, Putra MFF, Jayusman SVA, Zulhilmi Z. Sustainable packaging: Bioplastics as a low—carbon future step for the sustainable development goals (SDGs). ASEAN J Sci Eng Mater. 2024; 3: 51-8.

[24]

Babayan—Mashhadi F, Rezvani—Noghani A, Mokaberi P, Amiri—Tehranizadeh Z, Saberi MR, Chamani J. Exploring the binding behavior mechanism of vitamin B12 to α—Casein and β—Casein: multi—spectroscopy and molecular dynamic approaches . J Biomol Struct Dyn. 2024; 42: 5995-6012.

[25]

Ma B, Al—Wraikat M, Shu Q, Yang X, Liu Y. An Overview of Interactions between Goat Milk Casein and Other Food Components: Polysaccharides, Polyphenols, and Metal Ions. Foods. 2024; 13: 2903.

[26]

Ke C, Liu B, Dudu OE, Zhang S, Meng L, Wang Y, et al. Modification of structural and functional characteristics of casein treated with quercetin via two interaction modes: Covalent and non—covalent interactions. Food Hydrocolloids. 2023; 137: 108394.

[27]

Carver JA, Holt C. Current concepts of casein and casein micelle structure, interactions, and dynamics. In: El—Bakry M, Mehta BM, editors. Casein. Academic Press; 2024. pp. 63-98.

[28]

Chen X, Fan R, Wang X, Zhang L, Wang C, Hou Z, et al. In vitro digestion and functional properties of bovine β—casein: A comparison between adults and infants . Food Res Int. 2024; 194: 114914.

[29]

Guyomarcʼh F, Héquet F, Féon SL, Leconte N, Garnier—Lambrouin F, Auberger J, et al. Life cycle inventory and life cycle impact assessment datasets of an industrial—scale milk fractionation process generating 5 co—products: Cream, casein, lactose and two whey—protein ingredients enriched in α—lactalbumin or β—lactoglobulin. Data Brief. 2024; 55: 110676.

[30]

van der Schaaf JM, Goulding DA, OʼRegan J, Affolter M, OʼMahony JA, Kelly AL. Proteolysis of lactoferrin and β—casein in complex coacervate and uncomplexed forms during in vitro infant gastrointestinal digestion . J Funct Foods. 2024; 116: 106141.

[31]

Fernández—Tomé S. Role of Food Digestion and Digestive System in the Nutritional, Functional and Health Properties of Food Bioactives. Nutrients. 2024; 16: 712.

[32]

Monaci L, Pilolli R, Quintieri L, Caputo L, Luparelli A, De Angelis E. Casein: allergenicity and molecular properties. In: El—Bakry M, Mehta BM, editors. Casein. Academic Press; 2024. pp. 363-82.

[33]

Balivo A, dʼErrico G, Genovese A. Sensory properties of foods functionalised with milk proteins. Food Hydrocolloids. 2024; 147: 109301.

[34]

García—Rojas V, Ríos—Moreno A, Hernández—Varela JD, Chanona—Pérez J, Valeriano—García N, Mora—Escobedo R. Image Texture and Confocal Study of Starch—Based Extrudates Reinforced with Vegetal and Animal Protein as Snack Alternatives. Microsc Microanal. 2025; 31: 2013—5.

[35]

Beigrezaei A, Rafipour R. Design of casein—based nanocarriers for targeted delivery of daunorubicin to leukemia cells. Biotechnol Appl Biochem. 2025; 72: 287-94.

[36]

Akintan OA, Gebremedhin KG, Uyeh DD. Linking Animal Feed Formulation to Milk Quantity, Quality, and Animal Health Through Data—Driven Decision—Making. Animals (Basel). 2025; 15: 162.

[37]

Nayik GA, Gull A, Masoodi L, Navaf M, Sunooj KV, Ucak İ, et al. Milk proteins: chemistry, functionality and diverse industrial applications. Cogent Food Agric. 2024; 10: 2377686.

[38]

Alrosan M, Tan T—C, Easa AM, Aluʼdatt MH, Tranchant CC, Almajwal AM, et al. Improving the Functionality of Lentil—Casein Protein Complexes through Structural Interactions and Water Kefir—Assisted Fermentation. Fermentation. 2023; 9: 194.

[39]

Ahmed J, Guler E, Ozcan GS, Cam ME, Homer—Vanniasinkam S, Edirisinghe M. Casein fibres for wound healing. J R Soc Interface. 2023; 20: 20230166.

[40]

Kolahreez D, Ghasemi—Mobarakeh L, Quartinello F, Liebner FW, Guebitz GM, Ribitsch D. Multifunctional Casein—Based Wound Dressing Capable of Monitoring and Moderating the Proteolytic Activity of Chronic Wounds. Biomacromolecules. 2024; 25: 700-14.

[41]

Xu Q, Xu X, Ma J, Zong Y, Yan K, Li P. "Casein micelle—nanoparticle double cross—linking" triggered stable adhesive, tough CA/MWCNT/PAAm hydrogel wearable strain sensors, for human motion monitoring. Int J Biol Macromol. 2023; 238: 124055.

[42]

Saha M, Dey S, Nawaz SM, Mallik A. Environment—friendly resistive memory based on natural casein: Role of electrode and bio—material concentration. Org Electron. 2023; 121: 106869.

[43]

Mao Y, Wang D, Hu J, Fu S. Mechanically flexible and flame retardant polyphenol—bridged casein/MXene composite for fire proofing repeatable contact/non—contact fire monitoring. Chem Eng J. 2023; 454: 140161.

[44]

Casein glue: What is casein glue?[Internet]. Agrocomplex Sp. z o.o.; c2025 [cited 2025 Jul 4]. Available from: https://agrocomplex.com.pl/blog/casein—glue/

[45]

3D Printing Milk(5/17/ 2017) [Internet]. [cited 2025 Jul 4]. Available from: https://www.chrisdagher.io/projects/milk

[46]

Ji S, Xu T, Liu Y, Li H, Luo J, Zou Y, et al. Investigation of the mechanism of casein protein to enhance 3D printing accuracy of cassava starch gel. Carbohydr Polym. 2022; 295: 119827.

[47]

Babul Reddy A, Manjula B, Sudhakar K, Sivanjineyulu V, Jayaramudu T, Sadiku ER. Polyethylene/Other Biomaterials—based Biocomposites and Bionanocomposites. Polyethylene—Based Biocompos Bionanocompos. 2016: 279-314.

[48]

Swaisgood HE. Review and update of casein chemistry. J Dairy Sci. 1993; 76: 3054-61.

[49]

Akers RM. A 100—Year Review: Mammary development and lactation . J Dairy Sci. 2017; 100: 10332-52.

[50]

Bingham EW, Farrell HM Jr. Phosphorylation of casein by the lactating mammary gland: a review. J Dairy Sci. 1977; 60: 1199-207.

[51]

McMahon DJ, Oommen BS. Casein Micelle Structure, Functions, and Interactions. In: McSweeney PLH, Fox PF, editors. Advanced Dairy Chemistry: Volume 1A: Proteins: Basic Aspects, 4th Edition. Boston, MA: Springer US; 2013. pp. 185-209.

[52]

Bengoechea C, Arrachid A, Guerrero A, Hill SE, Mitchell JR. Relationship between the glass transition temperature and the melt flow behavior for gluten, casein and soya. J Cereal Sci. 2007; 45: 275-84.

[53]

Kang Y, Jimenez—Flores R, Richardson T. Casein genes and genetic engineering of the caseins. Basic Life Sci. 1986; 37: 95-111.

[54]

Tyulkin SV, Vafin RR, Zagidullin LR, Akhmetov TM, Petrov AN, Diel F. Technological Properties of Milk of Cows with Different Genotypes of Kappa—Casein and Beta—Lactoglobulin. Foods Raw Mater. 2018; 6: 154-62.

[55]

Ramakrishnan M, Zhou X, Dydak U, Savaiano DA. Gastric Emptying of New—World Milk Containing A1 and A2 Β—Casein Is More Rapid as Compared to Milk Containing Only A2 Β—Casein in Lactose Maldigesters: A Randomized, Cross—Over Trial Using Magnetic Resonance Imaging. Nutrients. 2023; 15: 801.

[56]

de Jesus BAP, Echeverri LMS, Magalhães MLB, Silva GFD. Generation and characterization of avian IgY antibodies for detecting beta—casein A1 in bovine milk. Anal Biochem. 2023; 678: 115283.

[57]

Jiménez—Montenegro L, Mendizabal JA, Alfonso L, Urrutia O. DNA extraction procedures and validation parameters of a real—time PCR method to control milk containing only A2 β—casein. Food Control. 2022; 142: 109259.

[58]

Wusigale, Liang L, Luo Y. Casein and pectin: Structures, interactions, and applications. Trends Food Sci Technol. 2020; 97: 391-403.

[59]

Sun Y, Ding Y, Liu B, Guo J, Su Y, Yang X, et al. Recent advances in the bovine β—casein gene mutants on functional characteristics and nutritional health of dairy products: Status, challenges, and prospects. Food Chem. 2024; 443: 138510.

[60]

Juan B, Salama AAK, Serhan S, Such X, Caja G, Pont L, et al. β—Casein: type A1 and A2. In: El—Bakry M, Mehta BM, editors. Casein. Academic Press; 2024. pp. 99-121.

[61]

Mukesh M, Sodhi M. Genetic Uniqueness of Indian Native Cattle with Special Reference to Their A1/A2 Allelic Status. In: Pundir RK, Niranjan SK, Behl R, editors. Sustainable Utilization of Indigenous Animal Genetic Resources of India. Haryana: National Bureau of Animal Genetic Resources Karnal; 2013. pp. 55-60.

[62]

Gai N, Waldron DS, Uniacke—Lowe T, Li B, OʼRegan J, GouldinDA, et al. Influence of β—casein genotype on Cheddar cheese making and ripening. Int Dairy J. 2024; 149: 105824.

[63]

Şahin Semerci E, Ergin Zeren F, Demir E, Küçükçetin A, Balcıoğlu MS. Influence of different genotype combinations of β—lactoglobulin and β—casein in cow milk on physicochemical and sensory properties of stirred yoghurt. Int Dairy J. 2025; 160: 106099.

[64]

Gai N, Uniacke—Lowe T, OʼRegan J, Goulding DA, Kelly AL. Influence of β—casein genotype on physicochemical properties and functionality of bovine milk. J Dairy Sci. 2023; 106: 8357-67.

[65]

de Vasconcelos ML, Oliveira LMFS, Hill JP, Vidal AMC. Difficulties in Establishing the Adverse Effects of β—Casomorphin—7 Released from β—Casein Variants—A Review. Foods. 2023; 12: 3151.

[66]

Prasad MG, Gourkhede DP, Vidyarani HB, Shindhe B, Mishra BP, Wankhade PR, et al. Delving into the A1/A2 milk hypothesis: A comprehensive analysis of milk proteins and their impact on human health. Int J Vet Sci Anim Husbandry. 2024; 9: 594-605.

[67]

Smolenski G, Armstrong K, Trivedi M, Clarke A. BCM—7 release from processed dairy products containing measured amounts of beta—casein variants. Int Dairy J. 2025; 161: 106136.

[68]

Ng SW, Lu P, Rulikowska A, Boehm D, OʼNeill G, Bourke P. The effect of atmospheric cold plasma treatment on the antigenic properties of bovine milk casein and whey proteins. Food Chem. 2021; 342: 128283.

[69]

Maryniak NZ, Sancho AI, Nielsen SD, Larsen LB, Gao Y, Bøgh KL, et al. Enzymatic hydrolysis and extensive heat treatment induce distinct modifications of cowʼs and camel milk proteins of relevance for production of infant formula. LWT. 2024; 191: 115591.

[70]

Zeng J, Zou J, Yi H, He J, Zhao J, Zhu S, et al. Localization and antigenicity reduction of immunodominant conformational IgE epitopes on αs1—casein. Int J Biol Macromol. 2025; 285: 138278.

[71]

Gil MV, Gutiérrez—Díaz G, Higuero N, Palma E, Fernández—Rivera N, Parrón—Ballesteros J, et al. Targeting cowʼs milk allergy using hypoallergenic protein—polyphenol formulas: A proof of concept. Food Chem. 2025; 463: 141285.

[72]

Yousef NS, Abd—Elkader MH, El—Bialy EF. Composite Alternative Milk I: Evaluation of Chemical, Mineral and Vitamin Contents of the Composite Alternative Milk. J Food Dairy Sci. 2024; 15; 13-9.

[73]

Chang S, Condon B, Smith J, Nam S. Innovative Approach to Flame Retardant Cotton Fabrics with Phosphorus Rich Casein via Layer—by—Layer Processing. Int J Mater Sci Appl. 2019; 8: 81-9.

[74]

Esposito E, Drechsler M, Mariani P, Panico AM, Cardile V, Crascì L, et al. Nanostructured lipid dispersions for topical administration of crocin, a potent antioxidant from saffron (Crocus sativus L.) . Mater Sci Eng C Mater Biol Appl. 2017; 71: 669-77.

[75]

Zhang Y, Wang X, Zhu H, Chen B, Wang C, Pang X, et al. The effect of agar on rheological properties and thermal stability of rennet—induced casein micelle gel. Colloids Surf A Physicochem Eng Asp. 2024; 686: 133273.

[76]

Kaseke T, Jovanovic V, Wimmer L, Vasovic T, Mutic T, Acimovic J, et al. Polypropylene micro— and nanoplastics affect the digestion of cowʼs milk proteins in infant model of gastric digestion. Environ Pollut. 2025; 383: 126803.

[77]

Sarode AR, Sawale PD, Khedkar CD, Kalyankar SD, Pawshe RD. Casein and Caseinate: Methods of Manufacture. In: Caballero B, Finglas P, Toldra F, editors. The Encyclopedia of Food and Health. Oxford: Academic Press; 2016. pp. 676-82.

[78]

Bouvier JM, Collado M, Gardiner D, Scott M, Schuck P. Physical and rehydration properties of milk protein concentrates: comparison of spray—dried and extrusion—porosified powders. Dairy Sci Technol. 2013; 93: 387-99.

[79]

Dahbi L, Alexander M, Trappe V, Dhont JKG, Schurtenberger P. Rheology and structural arrest of casein suspensions. J Colloid Interface Sci. 2010; 342: 564—70.

[80]

Vijayan JG. Zein—Based Composites: Synthesis, Characterization Properties, and Applications. In: Foundation and Growth of Macromolecular Science. 1st ed. Apple Academic Press; 2023.

[81]

Swaisgood HE. Chemistry of the Caseins. In: Fox PF, McSweeney PLH, editors. Advanced Dairy Chemistry—1 Proteins: Part A / Part B. Boston, MA: Springer US; 2003. pp. 139-201.

[82]

Pérez—Fuentes L, Drummond C, Faraudo J, Bastos—González D. Adsorption of Milk Proteins (β—Casein and β—Lactoglobulin) and BSA onto Hydrophobic Surfaces . Materials (Basel). 2017; 10: 893.

[83]

El—Negoumy AM. Effect of Method of Preparing Iso—Electric Casein on Its Electrophoretic Properties. J Dairy Sci. 1963; 46: 768-73.

[84]

Hipp NJ, Groves ML, Custer JH, McMeekin TL. Separation of α—, β— and γ—Casein . J Dairy Sci. 1952; 35: 272-81.

[85]

Rose D, Davies DT, Yaguchi M. Quantitative Determination of the Major Components of Casein Mixtures by Column Chromatography on DEAE—Cellulose. J Dairy Sci. 1969; 52: 8-11.

[86]

Hollar CM, Law AJ, Dalgleish DG, Medrano JF, Brown RJ. Separation of beta—casein A1, A2, and B using cation—exchange fast protein liquid chromatography . J Dairy Sci. 1991; 74: 3308—13.

[87]

Aimutis WR, Eigel WN. Identification of λ—Casein as Plasmin—Derived Fragments of Bovine αs1—Casein . J Dairy Sci. 1982; 65: 175-81.

[88]

Abbas A, Issa A, Tayib NN, Jubrael J. Kappa—Casein Gene (CSN3) Polymorphisms Detection in Three Indigenous Iraqi Goat Breeds, Using PCR—RFLP and SNP Markers. Egypt J Vet Sci. 2024; 55: 643-9.

[89]

Yaguchi M, Davies DT, Kim YK. Preparation of κ—Casein by Gel Filtration. J Dairy Sci. 1968; 51: 473—7.

[90]

Sweett H, Van Doormaal B. Selection for Milk Caseins: Beta and Kappa. Lactanet. 2022.

[91]

Chen C, Li Y, Yu H, Xu Z, Tian H, Yuan H. Mechanistic Insights into the interaction between aldehyde aroma compounds and β—Casein through Multi—Spectroscopy and molecular dynamics. Food Res Int. 2025; 200: 115451.

[92]

Singh MK, Kumar A, Nimmanapalli R, Hooda A. Probing of alpha, beta and kappa—caseins polymorphic variants in Gangatiri cow milk with the use of polyacrylamide gel electrophoresis and HRAMS. J Dairy Res. 2023; 90: 54-7.

[93]

Lei C, Wu X, Wang S, Gao A, Mu G, Qian F. Mechanism analysis of promoting calcium absorption and bone formation of peptides from different casein fractions. Food Biosci. 2024; 58: 103728.

[94]

Kerr CM, Schneider OL, Tichy S, Huge BJ, Champion MM. Capillary Isoelectric Focusing of Proteins and Peptides Using an In—Line cIEF—ESI Interface with Improved MS Characteristics. Anal Chem. 2025; 97: 649-57.

[95]

Kaimala S, Kumar S. An evolutionarily conserved non—coding element in casein locus acts as transcriptional repressor. Gene. 2015; 554: 75-80.

[96]

Wen A, Yuan S, Wang H, Mi S, Yu H, Guo Y, et al. Molecular insights on the binding of chlortetracycline to bovine casein and its effect on the thermostability of chlortetracycline. Food Chem. 2024; 432: 137104.

[97]

Ghadamgahi Z, Motavalizadehkakhky A, Mehrzad J, Amiri—Tehranizadeh Z, Chamani J. Probing the interaction behavior of Nano—Resveratrol with α—lactalbumin in the presence of β—lactoglobulin and β—casein: spectroscopy and molecular simulation studies. J Biomol Struct Dyn. 2024;[Epub ahead of print].

[98]

Burgain J, Gaiani C, Cailliez—Grimal C, Jeandel C, Scher J. Encapsulation of Lactobacillus rhamnosus GG in microparticles: Influence of casein to whey protein ratio on bacterial survival during digestion . Innovative Food Sci Emerging Technol. 2013; 19: 233—42.

[99]

Condict L, Elliott S, Hung A, Ashton J, Kasapis S. Interfacing β—casein—Phenolic compound interactions via molecular dynamics simulations with diffusion kinetics in delivery vehicles . Food Chem. 2024; 435: 137595.

[100]

Casein[Internet]. [cited 2025 Jul 4]. Available from: https://en.wikipedia.org/wiki/Casein

[101]

Du Z, Xu N, Yang Y, Li G, Tai Z, Li N, et al. Study on internal structure of casein micelles in reconstituted skim milk powder. Int J Biol Macromol. 2023; 224: 437-52.

[102]

Villa C, Costa J, Oliveira MBPP, Mafra I. Bovine Milk Allergens: A Comprehensive Review. Compr Rev Food Sci Food Saf. 2018; 17: 137-64.

[103]

McMahon DJ. Letter to the editor: The dynamic casein supramolecule: A response to Horne (2010) . J Dairy Sci. 2010; 93: 3404.

[104]

Lee EY, Lee WH, Kaetzel CS, Parry G, Bissell MJ. Interaction of mouse mammary epithelial cells with collagen substrata: regulation of casein gene expression and secretion. Proc Natl Acad Sci U S A. 1985; 82: 1419-23.

[105]

Lorenzen M, van den Berg FWJ, Lillevang SK, Ahrné L. The effect of milk fat content on microstructure and rheological properties of rennet casein gel emulsions. Food Hydrocolloids. 2024; 146: 109243.

[106]

de Groot A, Bijl E, Sagis LMC. Casein network formation at oil—water interfaces is reduced by β—casein and increased by Ca2+ . Food Hydrocolloids. 2025; 160: 110741.

[107]

Zhang C, Chu H, Gao L, Hou Z, He J, Wang C, et al. Encapsulation of Lactiplantibacillus plantarum with casein—gellan gum emulsions to enhance its storage, pasteurization, and gastrointestinal survival . Food Chem. 2025; 462: 140909.

[108]

Chang C, Zong M, Teng Y, Zeng X, Guo Y, Pan D, et al. Preparation and characterisation of novel casein—gum Arabic composite microcapsules for targeted in vivo delivery of Lactiplantibacillus plantarum A3 . Benef Microbes. 2024; 15: 51-66.

[109]

Zulewska J, Barbano DM. Influence of casein on flux and passage of serum proteins during microfiltration using polymeric spiral—wound membranes at 50°C. J Dairy Sci. 2013; 96: 2048-60.

[110]

Thienel KJF, Holder A, Schubert T, Boom RM, Hinrichs J, Atamer Z. Fractionation of milk proteins on pilot scale with particular focus on β—casein. Int Dairy J. 2018; 79: 73-7.

[111]

Post AE, Arnold B, Weiss J, Hinrichs J. Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of αS— and β—casein . J Dairy Sci. 2012; 95: 1603-16.

[112]

Reiter M, Berry B, Reitmaier M, Kulozik U. Tailoring acid gelation functionality of micellar casein concentrate: Impact of combining microfluidization and calcium chelation on gel firmness and serum binding. J Food Eng. 2025; 391: 112414.

[113]

van der Schaaf JM, Goulding DA, Fuerer C, OʼRegan J, OʼMahony JA, Kelly AL. A novel approach to isolation of β—casein from micellar casein concentrate by cold microfiltration combined with chymosin treatment. Int Dairy J. 2024; 148: 105796.

[114]

Zhang J, Vincenzetti S, Polidori P, Polzonetti V, Michele AD, Perinelli DR, et al. The effects of pH, temperature, and buffer concentration on the self—assembling behavior, secondary structure, and surface hydrophobicity of donkey and bovine β—casein. Food Chem. 2024; 433: 137285.

[115]

Daniloski D, Markoska T, McCarthy NA, Vasiljevic T. Casein micelle with different β—casein phenotypes: Fingerprinting pH—induced structural changes using FTIR and NMR spectroscopies. Food Hydrocolloids. 2023; 143: 108881.

[116]

Perticaroli S, Nickels JD, Ehlers G, Mamontov E, Sokolov AP. Dynamics and rigidity in an intrinsically disordered protein, β—casein. J Phys Chem B. 2014; 118: 7317—26.

[117]

Augustin MA, Sanguansri L. Encapsulation of Bioactives. In: Aguilera JM, Lillford PJ, editors. Food Materials Science: Principles and Practice. New York, NY: Springer New York; 2008. pp. 577-601.

[118]

Antuma LJ, Steiner I, Garamus VM, Boom RM, Keppler JK. Engineering artificial casein micelles for future food: Is casein phosphorylation necessary? Food Res Int. 2023; 173: 113315.

[119]

Che J, Fan Z, Bijl E, Thomsen JPS, Mijakovic I, Hettinga K. Unravelling the dominant role of phosphorylation degree in governing the functionality of reassembled casein micelles: Implications for future dairy production through precision fermentation. Food Hydrocolloids. 2025; 159: 110615.

[120]

Holt C, Sawyer L. Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the αS1—, β— and κ—caseins . J Chem Soc, Faraday Trans. 1993; 89: 2683—92.

[121]

Horne DS, Dalgleish DG. A photon correlation spectroscopy study of size distributions of casein micelle suspensions. Eur Biophys J. 1985; 11: 249—58.

[122]

Deshwal GK, Gómez—Mascaraque LG, Fenelon M, Huppertz T. A Review on the Effect of Calcium Sequestering Salts on Casein Micelles: From Model Milk Protein Systems to Processed Cheese. Molecules. 2023; 28: 2085.

[123]

Rodzik A, Król—Górniak A, Railean V, Sugajski M, Gołębiowski A, Horne DS, et al. Study on zinc ions binding to the individual casein fractions: αS1—, β— and κ—casein . J Mol Struct. 2023; 1272: 134251.

[124]

Dalgleish DG. Sedimentation of Casein Micelles During the Storage of Ultra—High Temperature Milk Products—a Calculation. J Dairy Sci. 1992; 75: 371-9.

[125]

Lin SH, Leong SL, Dewan RK, Bloomfield VA, Morr CV. Effect of calcium ion on the structure of native bovine casein micelles. Biochemistry. 1972; 11: 1818-21.

[126]

Hettiarachchi CA, Swulius MT, Harte FM. Assessing constituent volumes and morphology of bovine casein micelles using cryo—electron tomography. J Dairy Sci. 2020; 103: 3971—9.

[127]

Choi J, Horne DS, Lucey JA. Determination of molecular weight of a purified fraction of colloidal calcium phosphate derived from the casein micelles of bovine milk. J Dairy Sci. 2011; 94: 3250-61.

[128]

Rose D. Relation Between Micellar and Serum Casein in Bovine Milk. J Dairy Sci. 1968; 51: 1897-902.

[129]

Nadugala BH, Hepworth G, Mazzonetto M, Nebl T, Pagel CN, Raynes JK, et al. Effect of composition, casein genetic variants and glycosylation degree on bovine milk whipping properties. Food Res Int. 2024; 179: 113949.

[130]

Dalgleish DG. Casein Micelles as Colloids: Surface Structures and Stabilities. J Dairy Sci. 1998; 81: 3013—8.

[131]

Tuinier R, de Kruif CG. Stability of casein micelles in milk. J Chem Phys. 2002; 117: 1290-5.

[132]

Pepper L, Farrell HM Jr. Interactions Leading to Formation of Casein Submicelles. J Dairy Sci. 1982; 65: 2259—66.

[133]

de Kruif CG, Huppertz T, Urban VS, Petukhov AV. Casein micelles and their internal structure. Adv Colloid Interface Sci. 2012; 171—172: 36-52.

[134]

Hiep HM, Endo T, Kerman K, Chikae M, Kim DK, Yamamura S. A localized surface plasmon resonance based immunosensor for the detection of casein in milk. Sci Technol Adv Mater. 2007; 8: 331— 8.

[135]

Jang HD, Swaisgood HE. Disulfide Bond Formation Between Thermally Denatured β—Lactoglobulin and κ—Casein in Casein Micelles. J Dairy Sci. 1990; 73: 900-4.

[136]

Holt C. Casein Micelle Substructure and Calcium Phosphate Interactions Studied by Sephacryl Column Chromatography. J Dairy Sci. 1998; 81: 2994-3003.

[137]

Liu Y, Guo R. The interaction between casein micelles and gold nanoparticles. J Colloid Interface Sci. 2009; 332: 265—9.

[138]

Novokshanova AL, Bilyalova AS, Aksenov IV. Spectrometric study of the interaction of phycocyanins with casein. AIP Conf Proc. 2023; 2777: 020027.

[139]

He Z, Zhang X, Qi W, Huang R, Su R. Alginate—casein microspheres as bioactive vehicles for nutrients. Trans Tianjin Univ. 2015; 21: 383-91.

[140]

Wang J, Su Y, Jia F, Jin H. Characterization of casein hydrolysates derived from enzymatic hydrolysis. Chem Cent J. 2013; 7: 62.

[141]

Gaiaschi A, Beretta B, Poiesi C, Conti A, Giuffrida MG, Galli CL, et al. Proteolysis of beta—casein as a marker of Grana Padano cheese ripening. J Dairy Sci. 2001; 84: 60-5.

[142]

Adoui F, Saadi S, Lemmadi S, Benelouezzane C, Guemra I, Boughellout H, et al. Unravelling the behaviour of camel milk caseins during hydrolysis and separation: Insights into proteomic profiles of caseins using high performance liquid chromatography and polyacrylamide gel electrophoresis. Food Humanity. 2025; 4: 100491.

[143]

Spagnolo S, Muckley ES, Ivanov IN, Hianik T. Analysis of trypsin activity at β—casein layers formed on hydrophobic surfaces using a multiharmonic acoustic method. Analyst. 2022; 147: 461—70.

[144]

Mahmoud MI, Malone WT, Cordle CT. Enzymatic Hydrolysis of Casein: Effect of Degree of Hydrolysis on Antigenicity and Physical Properties. J Food Sci. 1992; 57: 1223—9.

[145]

Favaro—Trindade CS, Santana AS, Monterrey—Quintero ES, Trindade MA, Netto FM. The use of spray drying technology to reduce bitter taste of casein hydrolysate. Food Hydrocolloids. 2010; 24: 336—40.

[146]

Mendanha DV, Molina Ortiz SE, Favaro—Trindade CS, Mauri A, Monterrey—Quintero ES, Thomazini M. Microencapsulation of casein hydrolysate by complex coacervation with SPI/pectin. Food Res Int. 2009; 42: 1099-104.

[147]

Siqueira da Silva de Souza D, Augusto Peixoto Tartare V, da Silva Bega B, Zambuzi GC, Ribeiro TS, Ribeiro C, et al. The pH role in casein—carboxymethylcellulose nano/microparticles formation. Colloids Surf A Physicochem Eng Asp. 2024; 682: 132953.

[148]

Ren J, Liao M, Li K, Chen F, Hu X, Ma L, et al. The aggregation of casein micelles induced by Ca2+ during in vitro digestion: effects on the release of loaded anthocyanins . Food Funct. 2024; 15: 503— 15.

[149]

Shivaram SH, Saini R. Spray Drying—Assisted Fabrication Of Passive Nanostructures: From Milk Protein. In: Nanotechnology Applications in Dairy Science. 1st ed. Apple Academic Press; 2019.

[150]

Inada A, Sawao A, Takahashi K, Oshima T. Enhanced water dispersibility and Caco—2 cell monolayer permeability of quercetin by complexation with casein hydrolysate. J Food Sci. 2022; 87: 1174-83.

[151]

Sail HV, Jagdale AD, Thakur MR, Tupe RS. Structural and functional characterisation of Maillard reaction products from casein—acid hydrolysate—sugars model system using multi—spectroscopic approach. Int Dairy J. 2024; 149: 105838.

[152]

Costa C, Azoia NG, Coelho L, Freixo R, Batista P, Pintado M. Proteins Derived from the Dairy Losses and By—Products as Raw Materials for Non—Food Applications. Foods. 2021; 10: 135.

[153]

Donato L, Alexander M, Dalgleish DG. Acid gelation in heated and unheated milks: interactions between serum protein complexes and the surfaces of casein micelles. J Agric Food Chem. 2007; 55: 4160—8.

[154]

McMahon DJ, Brown RJ. Enzymic Coagulation of Casein Micelles: A Review. J Dairy Sci. 1984; 67: 919-29.

[155]

McMahon DJ, Du H, McManus WR, Larsen KM. Microstructural changes in casein supramolecules during acidification of skim milk. J Dairy Sci. 2009; 92: 5854-67.

[156]

Mellema M, Walstra P, van Opheusden JH, van Vliet T. Effects of structural rearrangements on the rheology of rennet—induced casein particle gels. Adv Colloid Interface Sci. 2002; 98: 25-50.

[157]

Udabage P, McKinnon IR, Augustin MA. Effects of mineral salts and calcium chelating agents on the gelation of renneted skim milk. J Dairy Sci. 2001; 84: 1569—75.

[158]

Cornale P, Renna M, Lussiana C, Chessa S, Mimosi A. Characterization of the Grey Goat of Lanzo Valleys (Fiurinà), a new Italian dairy population. In: International Goat Association, editor. Proceedings of XI International Conference on Goats; 2012 Sep 23—27; Gran Canaria, Spain. Las Palmas de Gran Canaria: International Goat Association; 2012. pp. 184.

[159]

Ambrosoli R, Stasio LD, Mazzocco P. Content of alpha S1—casein and coagulation properties in goat milk. J Dairy Sci. 1988; 71: 24-8.

[160]

Jung T, Hwang H, Yun S, Lee W, Kim J, Ahn J, et al. Hypoallergenic and Physicochemical Properties of the A2 β—Casein Fractionof Goat Milk. Korean J Food Sci Anim Resour. 2017; 37: 940-7.

[161]

Ye H, Yu W. Different influences of dietary fiber from various sources on the in vitro digestibility of casein as uncovered by the study of protein—dietary fiber interactions . Food Res Int. 2024; 176: 113845.

[162]

Wang T, Chen J, Zhong Y, Xu D, Ren D. Investigating the role of lemon peel fiber in the casein gelation mechanism of low—fat yogurt. Food Hydrocolloids. 2025; 160: 110862.

[163]

Hassan B, Chatha SAS, Hussain AI, Zia KM, Akhtar N. Recent advances on polysaccharides, lipids and protein based edible films and coatings: A review. Int J Biol Macromol. 2018; 109: 1095—107.

[164]

Ranadheera CS, Liyanaarachchi WS, Chandrapala J, Dissanayake M, Vasiljevic T. Utilizing unique properties of caseins and the casein micelle for delivery of sensitive food ingredients and bioactives. Trends Food Sci Technol. 2016; 57: 178-87.

[165]

Sordo F, Janecek E, Qu Y, Michaud V, Stellacci F, Engmann J, et al. Microstructured Fibers for the Production of Food. Adv Mater. 2019; 31: e1807282.

[166]

Nickerson M, Yan C, Cloutier S, Zhang W. Chapter 37 — Protection and Masking of Omega—3 and —6 Oils via Microencapsulation. In: Gaonkar AG, Vasisht N, Khare AR, Sobel R, editors. Microencapsulation in the Food Industry. San Diego: Academic Press; 2014. pp. 485-500.

[167]

Shi Y, Zhao C, Binghui MA, Huang A. Development of edible casein. China Dairy Ind. 2017.

[168]

Yu Q, Wu H, Fan L. Formation of casein and maltodextrin conjugates using shear and their effect on the stability of total nutrient emulsion based on homogenization. Food Hydrocolloids. 2024; 149: 109533.

[169]

Bhatia S, Shah YA, Al—Harrasi A, Jawad M, Koca E, Aydemir LY. Novel applications of black pepper essential oil as an antioxidant agent in sodium caseinate and chitosan based active edible films. Int J Biol Macromol. 2024; 254: 128045.

[170]

Kuerman M, Shi R, Zhang Y, Liu Y, Hou B, Li B. Lactiplantibacillus plantarum strains with proteolytic abilities showed diverse effects on casein gel formation during fermentation . Food Hydrocolloids. 2024; 148: 109406.

[171]

Lu Z, Sheng Z, Zhou H, He J, Zhang X, Zhang Y. Improvement of casein/κ—carrageenan composite gel properties: Role of locust bean gum concentration. Food Hydrocolloids. 2025; 158: 110547.

[172]

Ma J, Lee J, Han SS, Oh KH, Nam KT, Sun J. Highly Stretchable and Notch—Insensitive Hydrogel Based on Polyacrylamide and Milk Protein. ACS Appl Mater Interfaces. 2016; 8: 29220—6.

[173]

Zad Bagher Seighalani F, McMahon DJ, Sharma P. Determination of critical gel—sol transition point of Highly Concentrated Micellar Casein Concentrate using multiple waveform rheological technique. Food Hydrocolloids. 2021; 120: 106886.

[174]

Nassar KS, Bayomy HM, Alamri ES, Ozaybi NA, Korma SA, Lv J, et al. Impact of high—pressure treatments on physicochemical and structural changes of reconstituted micellar casein concentrates from bovine and caprine milk: A comparative study. J Dairy Sci. 2025; 108: 206-17.

[175]

Yin W, Su R, Qi W, He Z. A casein—polysaccharide hybrid hydrogel cross—linked by transglutaminase for drug delivery. J Mater Sci. 2012; 47: 2045—55.

[176]

Yi J, Li Y, Yang L, Zhang LM. Kinetics and thermodynamics of adsorption of Cu2+ and methylene blue to casein hydrogels . J Polym Res. 2019; 26: 235.

[177]

Narskii AR. Investigations of protein casein adhesives in 1927—1934 in research works of Central Aerohydrodynamic Institute and All—Russia Institute of the Aircraft Materials. Polym Sci Ser D. 2010; 3: 217-21.

[178]

Silva GA, Vaz CM, Coutinho OP, Cunha AM, Reis RL. In vitro degradation and cytocompatibility evaluation of novel soy and sodium caseinate—based membrane biomaterials. J Mater Sci Mater Med. 2003; 14: 1055-66.

[179]

Shchipunov Y, Shipunova N. Regulation of silica morphology by proteins serving as a template for mineralization. Colloids Surf B Biointerfaces. 2008; 63: 7-11.

[180]

Carr A, Golding M. Functional Milk Proteins Production and Utilization: Casein—Based Ingredients. In: McSweeney PLH, OʼMahony JA, editors. Advanced Dairy Chemistry: Volume 1B: Proteins: Applied Aspects. New York, NY: Springer New York; 2016. pp. 35-66.

[181]

Zhou C, Zhang D, Bai Y, Li S. Casein phosphopeptide—amorphous calcium phosphate remineralization of primary teeth early enamel lesions. J Dent. 2014; 42: 21-9.

[182]

Rajendran R, Kunjusankaran RN, Sandhya R, Anilkumar A, Santhosh R, Patil SR. Comparative Evaluation of Remineralizing Potential of a Paste Containing Bioactive Glass and a Topical Cream Containing Casein Phosphopeptide—Amorphous Calcium Phosphate: An in Vitro Study. Pesqui Bras Odontopediatria Clín Integr. 2019; 19: 1-10.

[183]

Markovic E, Peric T, Kojic S, Stosic M, Scepan I, Petrovic B. Influence of casein phosphopeptide—amorphous calcium phosphate on the surface topography and composition of nickel—titanium archwires during orthodontic treatment with fixed appliances. J Oral Sci. 2024; 66: 60-5.

[184]

Rathod P, Mankar N. Comparative evaluation of fracture resistance of re—attached teeth using self—adhesive bioactive flowable composite after preconditioning the fractured coronal fragments with different remineralizing agents. F1000Research. 2023; 12: 791.

[185]

Wei X, Wen X, Zheng H, Zhang Y, Jia Q. Facile synthesis of Fe3+ immobilized magnetic polydopamine—polyethyleneimine composites for phosphopeptide enrichment . J Chromatogr A. 2024; 1719: 464752.

[186]

Lee J, Lee JH, Paik SR, Yeom B, Char K. Thermally triggered self—assembly of κ—casein amyloid nanofibrils and their nanomechanical properties. Polymer. 2019; 179: 121626.

[187]

Miyake M, Kim D, Hata T. Casein—assisted enhancement of the compressive strength of biocemented sand. Sci Rep. 2022; 12: 12754.

[188]

Khakalo A, Filpponen I, Rojas OJ. Protein—mediated interfacial adhesion in composites of cellulose nanofibrils and polylactide: Enhanced toughness towards material development. Compos Sci Technol. 2018; 160: 145-51.

[189]

Fortunati E, Luzi F, Yang W, Kenny JM, Torre L, Puglia D. Chapter 4 — Bio—Based Nanocomposites in Food Packaging. In: Cerqueira MÂPR, Lagaron JM, Pastrana Castro LM, de Oliveira Soares Vicente AAM, editors. Nanomaterials for Food Packaging. Elsevier; 2018. pp. 71-110.

[190]

Husnayain N, Adi P, Mulyani R, Tsai SY, Chang CK, Punthi F, et al. Active Packaging of Chitosan—casein Phosphopeptide Modified Plasma—treated LDPE for CO2 Regulation to Delay Texture Softening and Maintain Quality of Fresh—cut Slice Persimmon During Storage . Food Bioprocess Technol. 2025; 18: 5532-48.

[191]

Xie J, Hsieh YL. Ultra—high surface fibrous membranes from electrospinning of natural proteins: casein and lipase enzyme. J Mater Sci. 2003; 38: 2125-33.

[192]

Sharma D, Ziegler GR, Harte FM. Ethanol—mediated electrospinning of casein—only bead—free nanofibers. Food Hydrocolloids. 2024; 148: 109503.

[193]

Chang SC, Condon B, Nam S. Development of Flame—Resistant Cotton Fabrics with Casein Using Pad—dry—cure and Supercritical Fluids Methods. Int J Mater Sci Appl. 2020; 9: 53-61.

[194]

Li B, Zhang Y, Abu Bakar A, Mohamad Z, Zhang J. Effects of ammonium polyphosphate and casein on the properties of poly (lactic acid). Fire Mater. 2023; 47: 1024—32.

[195]

Zhang X, Guan Q, Ding S, Wang Z, Xie H. Enhanced thermal stability, flame retardancy, and mechanical properties of casein—modified rigid polyurethane foams. Case Stud Therm Eng. 2025; 69: 106039.

[196]

Viraneva A, Marudova M, Milenkova S, Grigorov A, Yovcheva T. Investigation of Polyelectrolyte Multilayers Deposited on Biodegradable Corona—Charged Substrates Used as Drug Delivery Systems. Coatings. 2024; 14: 85.

[197]

Liu S, Yu H, Huang K. Structural characteristics and biocompatibility of a casein—based nanocomposite for potential biomedical applications. J Mater Sci. 2018; 53: 3959-71.

[198]

Chick J, Ustunol Z. Mechanical and barrier properties of lactic acid and rennet precipitated casein—based edible films. J Food Sci. 1998; 63: 1024-7.

[199]

Yao Y, Wang H, Wang R, Chai Y. Preparation and characterization of homogeneous and enhanced casein protein—based composite films via incorporating cellulose microgel. Sci Rep. 2019; 9: 1221.

[200]

Biranje SS, Sun J, Cheng L, Cheng Y, Shi Y, Yu S, et al. Development of Cellulose Nanofibril/Casein—Based 3D Composite Hemostasis Scaffold for Potential Wound—Healing Application. ACS Appl Mater Interfaces. 2022; 14: 3792-808.

[201]

Cubides YTP, Eklund PR, Foegeding EA. Casein as a Modifier of Whey Protein Isolate Gel: Sensory Texture and Rheological Properties. J Food Sci. 2019; 84: 3399-410.

[202]

Smith GA, Friedman M. Effect of Carbohydrates and Heat on the Amino Acid Composition and Chemically Available Lysine Content of Casein. J Food Sci. 1984; 49: 817—20.

[203]

Beaulieu M, Pouliot Y, Pouliot M. Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios. J Food Sci. 1999; 64: 776-80.

[204]

Rodzik A, Pomastowski P, Sagandykova GN, Buszewski B. Interactions of Whey Proteins with Metal Ions. Int J Mol Sci. 2020; 21: 2156.

[205]

Donato L, Guyomarcʼh F. Formation and properties of the whey protein/κ—casein complexes in heated skim milk—A review. Dairy Sci Technol. 2009; 89: 3-29.

[206]

Carter BG, Cheng N, Kapoor R, Meletharayil GH, Drake MA. Invited review: Microfiltration—derived casein and whey proteins from milk . J Dairy Sci. 2021; 104: 2465-79.

[207]

Lundén A, Nilsson M, Janson L. Marked effect of beta—lactoglobulin polymorphism on the ratio of casein to total protein in milk. J Dairy Sci. 1997; 80: 2996-3005.

[208]

Luccia AD, Picariello G, Trani A, Alviti G, Loizzo P, Faccia M, et al. Occurrence of beta—casein fragments in cold—stored and curdled river buffalo (Bubalus bubalis L.) milk . J Dairy Sci. 2009; 92: 1319-29.

[209]

Swaminathan AV, Lillevang SK, Govindasamy—Lucey S, Jaeggi JJ, Johnson ME, Lucey JA. Impact of pre—acidification on the functionality and insoluble calcium levels of low—moisture part—skim mozzarella made from high—casein milk. J Dairy Sci. 2025; 105: 173-89.

[210]

Ma S, Ye A, Singh H, Acevedo—Fani A. Heat—induced interactions between microfluidized hemp protein particles and caseins or whey proteins. Food Chem. 2025; 463: 141290.

[211]

Lorenzen M, Tică A, van den Berg FWJ, Lillevang SK, WindhaEJ, Ahrné L. The effect of nitrogen injection on the structure and textural properties of casein—based extrudates. Food Hydrocolloids. 2025; 164: 111142.

[212]

Wen A, Chen Y, Yuan S, Yu H, Guo Y, Cheng Y, et al. Elucidation of the binding behavior between tetracycline and bovine casein by multi—spectroscopic and molecular simulation methods. J Lumin. 2023; 260: 119879.

[213]

Shen S, Liu X, Tang D, Yang H, Cheng J. Digestive characteristics of astaxanthin oil in water emulsion stabilized by a casein—caffeic acid—glucose ternary conjugate. Food Chem. 2024; 438: 138054.

[214]

Allasia M, Mancilla A, Ronco LI, Passeggi MCG Jr, Gugliotta LM, Minari RJ. Efficient incorporation of protein into waterborne hybrid acrylic based nanoparticles. Prog Org Coat. 2024; 188: 108171.

[215]

Solera—Sendra J, Ballard N, Valle LJD, Franco L. Recent Advances in Combining Waterborne Acrylic Dispersions with Biopolymers. Polymers (Basel). 2025; 17: 1027.

[216]

Arjmandi S, Kheiri A, Kazemzadeh M, Falamaki C. Casein/starch composites: novel binders for green carbonaceous electrodes applied in the capacitive deionization of water. New J Chem. 2024; 48: 654—63.

[217]

Shuba A, Kuchmenko T, Ruslan U, Ekaterina B. Composite Coatings of Piezoelectric Quartz Sensors Based on Viscous Sorbents and Casein Micelles. Int J Electron Commun Eng. 2024; 18: 1-4.

[218]

Lin X, Li Y, Qi B, Zhang S, Li X. Casein—phosphatidylcholine emulsifier remodels LPS—induced intestinal barrier disfunction via regulating ferroptosis and lipid metabolism. Int J Biol Macromol. 2024; 254: 127595.

[219]

Vaz CM, Fossen M, van Tuil RF, de Graaf LA, Reis RL, Cunha AM. Casein and soybean protein—based thermoplastics and composites as alternative biodegradable polymers for biomedical applications. J Biomed Mater Res A. 2003; 65: 60-70.

[220]

Ptiček Siročić A, Kratofil Krehula L, Katančić Z, Hrnjak—Murgić Z. Characterization of Casein Fractions — Comparison of Commercial Casein and Casein Extracted from Cowʼs Milk. Chem Biochem Eng Q. 2017; 30: 501-9.

[221]

Santhosh Kumar B, Hemalatha T, Deepachitra R, Narasimha Raghavan R, Prabu P, Sastry TP. Biphasic calcium phosphate—casein bone graft fortified with Cassia occidentalis for bone tissue engineering and regeneration . Bull Mater Sci. 2015; 38: 259-66.

[222]

Bier MC, Kohn S, Stierand A, Grimmelsmann N, Homburg SV, Rattenholl A, et al. Investigation of eco—friendly casein fibre production methods. IOP Conf Ser: Mater Sci Eng. 2017; 254: 192004.

[223]

Hassabo AG, Khaleed N, Shaker S, Abd El—Salam NA, Mohamed NA, Gouda NZ, et al. Significance of casein fiber in textile technology. J Text Color Polym Sci. 2024; 21: 63-73.

[224]

Khan MA, Hemar Y, Li J, Yang Z, De Leon—Rodriguez LM. Fabrication, characterization, and potential applications of re—assembled casein micelles. Crit Rev Food Sci Nutr. 2023; 64: 7916-40.

[225]

Ucpinar Durmaz B, Aytac A. Poly (vinyl alcohol) and casein films: The effects of glycerol amount on the properties of films. Res Eng Struct Mat. 2019; 5: 155-65.

[226]

Sali SS, Gould ML, Qasim M, Ali MA. Biodegradable methacrylated casein for cardiac tissue engineering applications. J Mater Chem B. 2021; 9: 1557-67.

[227]

Brzyski P, Pietrak K, Cieślikiewicz Ł, Łapka P. Hygrothermal and Mechanical Characterization of Hemp Concrete Modified with Acid Casein Admixture. J Mater Civ Eng. 2025; 37: 04025116.

[228]

Movahedi M, Orash Mahmoud Salehi A, hajipour FP, Etemad S. Casein release and characterization of electrospun nanofibres for cartilage tissue engineering. Bull Mater Sci. 2022; 45: 76.

[229]

Antuma LJ, Braitmaier SH, Garamus VM, Hinrichs J, Boom RM, Keppler JK. Engineering artificial casein micelles for future food: Preparation rate and coagulation properties. J Food Eng. 2024; 366: 111868.

[230]

Zhang F, Ma J, Xu Q, Zhou J, Simion D, Carmen G, et al. Hollow Casein—Based Polymeric Nanospheres for Opaque Coatings. ACS Appl Mater Interfaces. 2016; 8: 11739-48.

[231]

Sinha S. Textile wastewater clarification using milk based formulations as an effective dye absorbent and flocculant. Mater Today: Proc. 2022; 67; 1304—9.

[232]

Kaseke T, Lujic T, Velickovic TC. Nano— and Microplastics Migration from Plastic Food Packaging into Dairy Products: Impact on Nutrient Digestion, Absorption, and Metabolism. Foods. 2023; 12: 3043.

[233]

Lai EPC, Onomhante A, Tsopmo A, Hosseinian F. Determination of polystyrene nanospheres and other nanoplastics in water via binding with organic dyes by capillary electrophoresis with laser—induced fluorescence detection. Talanta. 2025; 284: 127265.

[234]

Huang Z, Chen C, Liu Y, Liu S, Zeng D, Yang C, et al. Influence of protein configuration on aggregation kinetics of nanoplastics in aquatic environment. Water Res. 2022; 219: 118522.

[235]

Galante R, Cunha F, Fangueiro R. Chapter 19 — Extraction and properties of casein biopolymer from milk. In: Sreekala MS, Ravindran L, Goda K, Thomas S, editors. Handbook of Natural Polymers. Elsevier; 2023. pp. 471-87.

[236]

Dezhampanah H, Esmaili M. Milk Casein Coated Iron Oxide Nanoparticles As Superparamagnetic Core/Shell Carrier for Biomedical Areas. Russ J Phys Chem. 2023; 97: 702—13.

[237]

Haque S, Patra CR. Chapter 22 — Casein—based nanosystems for therapeutic applications. In: Hasnain MS, Nayak AK, Aminabhavi TM, editors. Polymeric Nanosystems. Academic Press; 2023. pp. 621—55.

[238]

Wang L, Jia W, Yang Q, Cai H, Zhao X. Casein nanoparticles as oral delivery carriers for improved bioavailability and hypoglycemic activity of apigenin. Food Hydrocolloids. 2024; 146: 109194.

[239]

Wang Y, Wang L, Liu R, Li X. Casein templated synthesis of porous perovskite and its application in visible—light photocatalytic degradation of methylene blue. Mater Sci Semicond Process. 2019; 103: 104597.

[240]

Li Y, Li O, Cao Z, Xu Y, Gong Y, Shi X. Fabrication of Uniform Casein/CaCO3 Vaterite Microspheres and Investigation of Its Formation Mechanism. Cryst Growth Des. 2017; 17: 6178—88.

[241]

Pan X, Yao P, Jiang M. Simultaneous nanoparticle formation and encapsulation driven by hydrophobic interaction of casein— graft—dextran and β—carotene . J Colloid Interface Sci. 2007; 315: 456-63.

[242]

Karaaslan MA, Gao G, Kadla JF. Nanocrystalline cellulose/β—casein conjugated nanoparticles prepared by click chemistry. Cellulose. 2013; 20: 2655-65.

[243]

Zhang Y, Song B, Wang X, Zhang W, Zhu H, Pang X. Rheological properties and microstructure of rennet—induced casein micelle/κ—carrageenan composite gels. LWT. 2023; 178: 114562.

[244]

Wu H, Qin J, Ji W, Palupi NW, Yang M. Interaction between curcumin and ultrafiltered casein micelles or whey protein, and characteristics of their complexes. J Food Sci. 2024; 89: 1582-98.

[245]

Wang XP, Wang CF, Zhao XQ, Ma MJ, Li ZH, Jiang H, et al. Comparison of milk protein concentrate, micellar casein, and whey protein isolate in loading astaxanthin after the treatment of ultrasound—assisted pH shifting. J Dairy Sci. 2024; 107: 141-54.

[246]

Zhao R, Torley P, Halley PJ. Emerging biodegradable materials: starch— and protein—based bio—nanocomposites. J Mater Sci. 2008; 43: 3058-71.

[247]

Fan H, Fu G, Feng S, He X, Cai W, Wan Y. Fabrication of casein—crocin nanocomplexes: Interaction mechanism, impact on stability and bioavailability of crocin. Food Hydrocolloids. 2023; 136: 108279.

[248]

Głąb TK, Boratyński J. Potential of Casein as a Carrier for Biologically Active Agents. Top Curr Chem (Cham). 2017; 375: 71.

[249]

Bachar M, Mandelbaum A, Portnaya I, Perlstein H, Even—Chen S, Barenholz Y, et al. Development and characterization of a novel drug nanocarrier for oral delivery, based on self—assembled β—casein micelles. J Control Release. 2012; 160: 164-71.

[250]

Cai J, Yan X, Liu X, Yin X, Shi A, Ji C, et al. Human β—casein—derived peptide BCCY—1 improved the intestinal barrier integrity by regulating the TLR4/eNOS/3—Nitrotyrosine axis. Food Chem. 2025; 463: 140821.

[251]

Akhtar A, Aslam S, Khan S, McClements DJ, Khalid N, Maqsood S. Utilization of diverse protein sources for the development of protein—based nanostructures as bioactive carrier systems: A review of recent research findings (2010—2021). Crit Rev Food Sci Nutr. 2023; 63: 2719-37.

[252]

Elzoghby AO, El—Fotoh WSA, Elgindy NA. Casein—based formulations as promising controlled release drug delivery systems. J Control Release. 2011; 153: 206-16.

[253]

Li Z, Jiang H, Guo M, Zhang Z, You X, Wang X, et al. Effect of various oligosaccharides on casein solubility and other functional properties: Via Maillard reaction. Int J Biol Macromol. 2024; 259: 129148.

[254]

Kajthunyakarn W, Sakloetsakun D, Pongjanyakul T. Sodium caseinate—magnesium aluminum silicate nanocomposite films for modified—release tablets. Mater Sci Eng C Mater Biol Appl. 2018; 92: 827—39.

[255]

Marcano RGV, Khalil NM, de Lurdes Felsner M, Mainardes RM. Mitigating amphotericin B cytotoxicity through gliadin—casein nanoparticles: Insights into synthesis, optimization, characterization, in vitro release and cytotoxicity evaluation. Int J Biol Macromol. 2024; 260: 129471.

[256]

Aljewicz M, Keklik M, Recio I, Martínez—Sanz M. Effect of polysaccharide—protein interactions on the multi—scale structure of hybrid micellar casein—xanthan gum systems. Food Hydrocolloids. 2024; 151: 109833.

[257]

Cañas—Sarazúa R, Briones—Labarca V, Giovagnoli—Vicuña C. Encapsulation of papaya seed oil in casein—alginate—based shell materials. Future Foods. 2024; 9: 100301.

[258]

Sáiz—Abajo M, González—Ferrero C, Moreno—Ruiz A, Romo—Hualde A, González—Navarro CJ. Thermal protection of β—carotene in re—assembled casein micelles during different processing technologies applied in food industry. Food Chem. 2013; 138: 1581—7.

[259]

Wang C, Chen X, Nakamura Y, Yu C, Qi H. Fucoxanthin activities motivate its nano/micro—encapsulation for food or nutraceutical application: a review. Food Funct. 2020; 11: 9338—58.

[260]

Yamamoto N, Akino A, Takano T. Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790 . J Dairy Sci. 1994; 77: 917—22.

[261]

Singh N, Gaur S. Investigating the Antioxidative and Antihypertensive Properties of Milk—Derived Bioactive Peptides Fermented by Lactic Acid Bacteria. Food Saf Health. 2025;[Epub ahead of print].

[262]

Elisha C, Bhagwat P, Pillai S. In silico and in vitro analysis of dipeptidyl peptidase—IV and angiotensin—converting enzyme inhibitory peptides derived from milk lactoferrin . Int Dairy J. 2025; 160: 106092.

[263]

Cetınkaya S, Akkaya B. Selective and single step adsorption of α—lactalbumin from whole cowʼs milk on hydroxyapatite microbeads. Mater Sci Eng C Mater Biol Appl. 2016; 68: 573—8.

[264]

Li K, Jiang P, Li S, Sun J, Qi C. ACE inhibitory casein peptide lowers blood pressure and reshapes gut microbiota in a randomized double blind placebo controlled trial. Sci Rep. 2025; 15: 13840.

[265]

Viora L, Tichané T, Nottelet B, Mouton J, Garric X, Berghe HVD, et al. Casein—based conjugates and graft copolymers. Synthesis, properties, and applications. Compr Rev Food Sci Food Saf. 2024; 23: e13306.

[266]

Alayoubi O, Poyraz Y, Hassan G, Gül SB, Çalhan N, Şahin NMM, et al. Hydrogels from Protein—Polymer Conjugates: A Pathway to Next—Generation Biomaterials. Gels. 2025; 11: 96.

[267]

Anedda R, Curti E. Innovation in Dairy Processes and Products: Exploring Recent Advances, Analytical Applications, and Reimagining Traditional Systems. Appl Sci. 2025; 15: 3770.

[268]

Robinson SR, Greenway FL, Deth RC, Fayet—Moore F. Effects of Different Cow—Milk Beta—Caseins on the Gut—Brain Axis: A Narrative Review of Preclinical, Animal, and Human Studies. Nutr Rev. 2025; 83: e1259-69.

[269]

Novika RGH, Sari AN, Nurhidayati S, Maulina R, Maulida LF, Wahidah NJ, et al. Effect of β—casein A2 cow milk supplementation on physical growth, inflammation, growth—related hormones, and nutritional biomarkers in stunted children. Ann Pediatr Endocrinol Metab. 2025; 30: 119-26.

[270]

El—Aidie SAM, Khalifa GSA. Innovative applications of whey protein for sustainable dairy industry: Environmental and technological perspectives—A comprehensive review. Compr Rev Food Sci Food Saf. 2024; 23: e13319.

PDF (1442KB)

17

Accesses

0

Citation

Detail

Sections
Recommended

/