1. OECD | Food and Agriculture Organization of the United Nations. OECD-FAO Agricultural Outlook 2025–2034. Paris: OECD Publishing; 2025, 166 p. https://doi.org/10.1787/601276cd-en
2. Ní Fhuaráin AM, O’Donnell CP, Luo J, Gowen AA. A review on MIR, NIR, fluorescence and Raman spectroscopy combined with chemometric modeling to predict the functional properties of raw bovine milk. ACS Food Science & Technology. 2024;4(10):2258–2271. https://doi.org/10.1021/acsfoodscitech.4c00130
3. Kartashova V. The dairy market of Russia shows growth. Animal Husbandry of Russia. 2025;(S2):2–5. (In Russ.) https://elibrary.ru/CNUOCJ
4. Khurshudyan SA, Blizkiy AM. Quality requirements for food waste. Production Quality Control. 2024;(1):27–30.
5. Shuvarikov AS, Yurova EA, Pastukh ON. Quality indicators of cow, goat and camel milk with account of allergenicity. Izvestiya of Timiryazev Agricultural Academy. 2017;(5):115–123. (In Russ.) https://doi.org/10.26897/0021-342X-2017-5-115-123
6. Donskaya GA. Antioxidant properties of milk and dairy products: Review. Food Industry. 2020;(12):86–91. (In Russ.) https://elibrary.ru/XNCFER
7. Nunes L, Tavares GM. Thermal treatments and emerging technologies: Impacts on the structure and techno-functional properties of milk proteins. Trends in Food Science & Technology. 2019;90:88–99. https://doi.org/10.1016/j.tifs.2019.06.004
8. Čurlej J, Zajác P, Čapla J, Golian J, Benešová L, et al. The effect of heat treatment on cow’s milk protein profiles. Foods. 2022;11(7):1023. https://doi.org/10.3390/foods11071023
9. Wang Y, Xiao R, Liu S, Wang P, Zhu Y, et al. The impact of thermal treatment intensity on proteins, fatty acids, macro/micro-nutrients, flavor, and heating markers of milk – a comprehensive review. International Journal of Molecular Sciences. 2024;25(16):8670. https://doi.org/10.3390/ijms25168670
10. Galstyan AG, Petrov AN, Illarionova EE, Semipyatniy VK, Turovskaya SN, et al. Effects of critical fluctuations of storage temperature on the quality of dry dairy product. Journal of Dairy Science. 2019;102(12):10779–10789. https://doi.org/10.3168/jds.2019-17229
11. Ebner J, Baum F, Pischetsrieder M. Identification of sixteen peptides reflecting heat and/or storage induced processes by profiling of commercial milk samples. Journal of Proteomics. 2016;147:66–75. https://doi.org/10.1016/j.jprot.2016.03.021
12. Arab M, Yousefi M, Khanniri E, Azari M, Ghasemzadeh-Mohammadi V, et al. A comprehensive review on yogurt syneresis: Effect of processing conditions and added additives. Journal of Food Science and Technology. 2023;60:1656–1665. https://doi.org/10.1007/s13197-022-05403-6
13. Akkerman M, Rauh VM, Christensen M, Johansen LB, Hammershøj M, et al. Effect of heating strategies on whey protein denaturation – revisited by liquid chromatography quadrupole time-of-flight mass spectrometry. Journal of Dairy Science. 2016;99(1):152–166. https://doi.org/10.3168/jds.2015-9924
14. Sharma A, Jana AH, Chavan RS. Functionality of milk powders and milk-based powders for end use applications – a review. Comprehensive Reviews in Food Science and Food Safety. 2012;11(5):518–528. https://doi.org/10.1111/j.1541-4337.2012.00199.x
15. Kruchinin AG, Illarionova EE, Bigaeva AV, Turovskaya SN. The role of dry milk technological properties in forming the quality of food systems. Bulletin of KSAU. 2020;(8):166–173. (In Russ.) https://doi.org/10.36718/1819-4036-2020-8-166-173
16. Bista A, Murphy EG, O’Donnell CP, O’Shea N. The effect of heat treatment on physicochemical properties of skim milk concentrate and spray-dried skim milk powder. International Journal of Dairy Technology. 2022;75(3):690–700. https://doi.org/10.1111/1471-0307.12876
17. Lindmark-Månsson H, Timgren A, Aldén G, Paulsson M. Two-dimensional gel electrophoresis of proteins and peptides in bovine milk. International Dairy Journal. 2005;15(2):111–121. https://doi.org/10.1016/j.idairyj.2004.06.010
18. Kruchinin AG, Bigaeva AV, Lazareva EG, Vafin RR, Mikhailova IYu, et al. Electrophoretic methods for study of protein systems. Dairy industry. 2020;(6):16–18. (In Russ.) https://doi.org/10.31515/1019-8946-2020-06-16-18
19. Barkovskaya IA, Turovskaya SN, Illarionova EE, Yaryshev VYu, Bliadze VG, et al. Comparison of IR and Raman spectroscopy methods for assessing structural changes in milk during heat treatment. Food Metaengineering. 2025;3(3):21–38. (In Russ.) https://doi.org/10.37442/fme.2025.3.91
20. Yurova EA, Zhizhin NA, Filchakova SA. Molecular genetic methods of analysis to identify the species affiliation of the raw material composition in food products. Vestnik of MSTU journal. 2020;23(3):214–223. https://doi.org/10.21443/1560-9278-2020-23-3-214-223
21. Khan AV, Lazareva EG, Fomenko OYu. Optimization of molecular genetic method for identification of dairy raw materials. Food Metaengineering. 2023;1(4):39–47. (In Russ.) https://doi.org/10.37442/fme.2023.4.29
22. Khan AV, Lazareva EG, Fomenko OYu. The problem of dairy products adulteration: analysis of the state and ways of resolution. Dairy industry. 2023;(5):54–56. https://doi.org/10.21603/1019-8946-2023-5-6
23. Koval DD, Khan AV, Lazareva EG, Fomenko OYu. Isolating bacterial DNA from goat milk and its products: comparative analysis. Food Processing: Techniques and Technology. 2025;55(2):390–399. (In Russ.) https://doi.org/10.21603/2074-9414-2025-2-2579
24. Losito I, Carbonara T, Monaci L, Palmisano F. Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: An investigation by liquid chromatography–electrospray ionization mass spectrometry. Analytical and Bioanalytical Chemistry. 2007;389:2065–2074. https://doi.org/10.1007/s00216-007-1447-0
25. Class L-C, Kuhnen G, Hanisch KL, Badekow S, Rohn S, et al. The shelf life of milk – a novel concept for the identification of marker peptides using multivariate analysis. Foods. 2024;13(6):831. https://doi.org/10.3390/foods13060831
26. Šebela M. Biomolecular profiling by MALDI-TOF mass spectrometry in food and beverage analyses. International Journal of Molecular Sciences. 2022;23(21):13631. https://doi.org/10.3390/ijms232113631
27. Kang W, Feng F, Zhou W, Jing M, Wang X, et al. Discrimination of overheated pasteurized milk using mass spectrometry-based proteomics. Journal of Chromatography B. 2024;1243:124236. https://doi.org/10.1016/j.jchromb.2024.124236
28. Panthi RR, Shibu SN, Ochalski TJ, O’Mahony JA. Raman spectra of micellar casein powders prepared with wet blending of glycomacropeptide and micellar casein concentrate. International Journal of Dairy Technology. 2023;76(2):429–435. https://doi.org/10.1111/1471-0307.12920
29. Zhang S, Zhang Z, Lin M, Vardhanabhuti B. Raman spectroscopic characterization of structural changes in heated whey protein isolate upon soluble complex formation with pectin at near neutral pH. Journal of Agricultural and Food Chemistry. 2012;60(48):12029–12035. https://doi.org/10.1021/jf303780c
30. Li C, Nielsen SB, Engholm-Keller K, Lund MN. Oxidation of whey proteins during thermal treatment characterized by a site-specific LC–MS/MS-based proteomic approach. Journal of Agricultural and Food Chemistry. 2022;70(14):4391–4406. https://doi.org/10.1021/acs.jafc.1c07946
31. Meltretter J, Wüst J, Pischetsrieder M. Modified peptides as indicators for thermal and nonthermal reactions in processed milk. Journal of Agricultural and Food Chemistry. 2014;62(45):10903–10915. https://doi.org/10.1021/jf503664y
32. Lu J, Zhu T, Dai Y, Xing L, Jinqi L, et al. The effect of heat treatment on the lactosylation of milk proteins. Journal of Dairy Science. 2023;106(12):8321–8330. https://doi.org/10.3168/jds.2023-23526
33. Kovalyov LI, Shishkin SS, Kovalyova MA, Ivanov AV, Vostrikova NL, et al. Proteomic research proteins in a sample of pork meat products. Vse o myase. 2013;(3):32–34. https://elibrary.ru/QCRSLF
34. Zvereva EA, Kovalev LI, Ivanov AV, Kovaleva MA, Zherdev AV, et al. Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products. Meat Science. 2015;105:46–52.
35. Alkadur MI, Pryanichnikova NS, Yurova EA, Petrov AN. Effect of thermal treatment and pasteurization on milk powder quality. Food Processing: Techniques and Technology. 2024;54(1):275–284. (In Russ.) https://doi.org/10.21603/2074-9414-2024-2-2506
36. 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(5):2023. https://doi.org/10.3390/molecules28052023
37. Krishna TC, Najda A, Bains A, Tosif MM, Papliński R, et al. Influence of ultra-heat treatment on properties of milk proteins. Polymers. 2021;13(18):3164. https://doi.org/10.3390/polym13183164
38. Li H, Zhao T, Li H, Yu J. Effect of heat treatment on the property, structure, and aggregation of skim milk proteins. Frontiers in Nutrition. 2021;8:714869. https://doi.org/10.3389/fnut.2021.714869
39. Mohammad-Beigi H, Wijaya W, Madsen M, Hayashi Y, Li R, et al. Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis. Food Hydrocolloids. 2023;137:108373. https://doi.org/10.1016/j.foodhyd.2022.108373
40. Zhang T, Liu Y, Cao J, Jiang L, Wang P, et al. Exploration of dynamic interaction between β-lactoglobulin and casein micelles during UHT milk process. International journal of biological macromolecules. 2024;277(Part 2):134367. https://doi.org/10.1016/j.foodhyd.2022.108373
41. Jovanovic S, Barac M, Macej O, Vucic T, Lacnjevac C. SDS-PAGE analysis of soluble proteins in reconstituted milk exposed to different heat treatments. Sensors. 2007;7(3):371–383. https://doi.org/10.3390/s7030371
42. Ichimura T, Kusaka M, Nakamura T. The effect of high-temperature heat treatment and homogenization on the microstructure of set yogurt curd networks. Journal of Dairy Research. 2023;90(3):306–311. https://doi.org/10.1017/S0022029923000523
43. Asaduzzaman M, Mahomud MS, Haque ME. Heat-induced interaction of milk proteins: Impact on yoghurt structure. International Journal of Food Science. 2021;2021:5569917. https://doi.org/10.1155/2021/5569917
44. Alkadur MI, Petrov AN, Pryanichnikova NS. Influence of the class of thermal treatment of dry milk on the structure and properties of the fermented curd. Food industry. 2024;(11):82–89. (In Russ.) https://doi.org/10.52653/PPI.2024.11.11.015
45. Wölk M, Milkovska-Stamenova S, Hoffmann R. Comprehensive profiling of the native and modified peptidomes of raw bovine milk and processed milk products. Foods. 2020;9(12):1841. https://doi.org/10.3390/foods9121841
46. Bhattacharya M, Salcedo J, Robinson RC, Henrick BM, Barile D. Peptidomic and glycomic profiling of commercial dairy products: Identification, quantification and potential bioactivities. npj Science of Food. 2019;3(1):4. https://doi.org/10.1038/s41538-019-0037-9
47. Ceballos LS, Morales ER, de la Torre Adarve G, Castro JD, Martínez LP, et al. Composition of goat and cow milk produced under similar conditions and analyzed by identical methodology. Journal of Food Composition and Analysis. 2009;22(4):322–329. https://doi.org/10.1016/j.jfca.2008.10.020
48. Holland JW, Gupta R, Deeth HC, Alewood PF. UHT milk contains multiple forms of αS1-casein that undergo degradative changes during storage. Food Chemistry. 2012;133(3):689–696. https://doi.org/10.1016/j.foodchem.2012.01.070
49. Freire P, Zambrano A, Zamora A, Castillo M. Thermal denaturation of milk whey proteins: A comprehensive review on rapid quantification methods being studied, developed and implemented. Dairy. 2022;3(3):500–512. https://doi.org/10.3390/dairy3030036
50. McMahon DJ, Oommen BS. Casein micelle structure, functions, and interactions. In: McSweeney P, Fox P, editors. Advanced Dairy Chemistry. Boston: Springer; 2013, pp. 185–209. https://doi.org/10.1007/978-1-4614-4714-6_6
51. Caroli AM, Savino S, Bulgari O, Monti E. Detecting β-casein variation in bovine milk. Molecules. 2016;21(2):141. https://doi.org/10.3390/molecules21020141
52. Kang Y, Jimenez-Flores R, Richardson T. Casein genes and genetic engineering of the caseins. In: Evans JW, Hollaender A, Wilson CM, editors. Genetic Engineering of Animals. Boston: Springer; 1986, pp. 95–111. https://doi.org/10.1007/978-1-4684-5110-8_9
53. Lai EPC, Tsopmo A. Casein chemistry–structure, functions, and applications. Exploratory Foods and Foodomics. 2025;3:101099. https://doi.org/10.37349/eff.2025.101099
54. Sava N, Van der Plancken I, Claeys W, Hendrickx M. The kinetics of heat-induced structural changes of β-lactoglobulin. Journal of Dairy Science. 2005;88(5):1646–1653. https://doi.org/10.3168/jds.S0022-0302(05)72836-8
55. Qasba PK, Kumar S. Molecular divergence of lysozymes and α-lactalbumin. Critical reviews in biochemistry and molecular biology. 1997;32(4):255–306. https://doi.org/10.3109/10409239709082574
56. Davies GJ, Williams SJ. Carbohydrate-active enzymes: Sequences, shapes, contortions and cells. Biochemical Society Transactions. 2016;44(1):79–87. https://doi.org/10.1042/BST20150186
57. Barkovskaya IA, Ryabova AE, Rozhkova IV. Complex modification of whey protein profile as an approach to the creation of enriched protein ingredients. Food systems. 2025;8(2):221–230. (In Russ.) https://doi.org/10.21323/2618-9771-2025-8-2-221-230
58. Clawin-Rädecker I, Kiesner C, Schlimme E. Analysis of the acid-soluble contents of α-lactalbumin, β-lactoglobulin, serum albumin and the immunoglobulin fraction in pasteurized milk. Kieler Milchwirtschaftliche Forschungsberichte. 2000;52(4):322–334. (In German)
59. Cho Y, Singh H, Creamer LK. Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system. Journal of Dairy Research. 2003;70(1):61–71. https://doi.org/10.1017/S0022029902005642
60. Paulsson M, Dejmek P. Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. Journal of Dairy Science. 1990;73(3):590–600. https://doi.org/10.3168/jds.S0022-0302(90)78707-3
61. Moriyama Y, Kondo N, Takeda K. Secondary structural changes of homologous proteins, lysozyme and α-lactalbumin, in thermal denaturation up to 130 °C and sodium dodecyl sulfate (SDS) effects on these changes: comparison of thermal stabilities of SDS-induced helical structures in these proteins. Langmuir. 2012;28(47):16268–16273. https://doi.org/10.1021/la3035598
62. Wu J, Chen S, Van der Meeren P. Heat stability assessment of milk: A review of traditional and innovative methods. Foods. 2024;13(14):2236. https://doi.org/10.3390/foods13142236
63. He H, Sun DW, Pu H, Chen L, Lin L. Applications of Raman spectroscopic techniques for quality and safety evaluation of milk: A review of recent developments. Critical Reviews in Food Science and Nutrition. 2019;59(5):770–793. https://doi.org/10.1080/10408398.2018.1528436
64. Vaskova H, Buckova M. Measuring the lactose content in milk. MATEC Web of Conferences. 2016;76:05011. https://doi.org/10.1051/matecconf/20167605011
65. Reiner J, Protte K, Hinrichs J. Investigation of the applicability of Raman spectroscopy as online process control during consumer milk production. ChemEngineering. 2020;4(3):45. https://doi.org/10.3390/chemengineering4030045
66. Choudhary S, Arora S, Kumari A, Narwal V, Sharma V. Effect of quality of milk on Maillard reaction and protein oxidation during preparation of cow and buffalo milk khoa. Journal of Food Science and Technology. 2017;54:2737–2745. https://doi.org/10.1007/s13197-017-2710-9
67. Silva MG, de Paula IL, Stephani R, Edwards HGM, de Oliveira LFC. Raman spectroscopy in the quality analysis of dairy products: A literature review. Journal of Raman Spectroscopy. 2021;52(12):2444–2478. https://doi.org/10.1002/jrs.6214
68. Sibono L, Tronci S, Hedegaard MAB, Errico M, Grosso M. Raman spectroscopy coupled with multivariate statistical process control for detecting anomalies during milk coagulation. Processes. 2025;13(11):3519. https://doi.org/10.3390/pr13113519
69. Yazgan NN, Genis HE, Bulat T, Topcu A, Durna S, et al. Discrimination of milk species using Raman spectroscopy coupled with partial least squares discriminant analysis in raw and pasteurized milk. Journal of the Science of Food and Agriculture. 2020;100(13):4756–4765. https://doi.org/10.1002/jsfa.10534