Dairy industry Dairy industry Молочная промышленность 1019-8946 97280 Информационный материал Information material Информационный материал Membrane Separation of Skim Milk: Proteins of Native Whey Protein Concentrate Мембранное фракционирование обезжиренного молока: протеины нативного концентрата сывороточных белков Володин Дмитрий Николаевич Volodin Dmitry N. info@dmprocess.ru

кандидат технических наук;

candidate of technical sciences;

 Топалов Виктор Константинович Topalov Victor K. info@dmprocess.ru Куликова Ирина Кирилловна Kulikova Irina K.

кандидат технических наук;

candidate of technical sciences;

 Семченко Анастасия Андреевна Semchenko Anastasiya A. https://orcid.org/0000-0002-5396-1548 Евдокимов Иван Алексеевич Evdokimov Ivan A. ievdokimov@ncfu.ru ООО «ДМП» Ставрополь Россия LLC "DMP" Stavropol Russian Federation ООО «ДМП» Ставрополь Россия LLC "DMP" Stavropol Russian Federation ООО «ДМП» Ставрополь Россия LLC "DMP" Stavropol Russian Federation ООО «ДМП» Ставрополь Россия LLC "DMP" Stavropol Russian Federation Северо-Кавказский федеральный университет Россия North-Caucasus Federal University Russian Federation 10 04 2025 10 04 2025 2 74 77 17 03 2025 31 03 2025 https://vestnik-bees.kemsu.ru/en/nauka/article/97280/view

Володин, Д. Н. Мембранное фракционирование обезжиренного молока: влияние казеина на формирование функциональных свойств белковых концентратов / Д. Н. Володин, В. К. Топалов, И. К. Куликова [и др.] // Молочная промышленность. 2024. № 6. С. 48–53. https://elibrary.ru/ihvtey Volodin, D. N. Membrannoe frakcionirovanie obezzhirennogo moloka: vliyanie kazeina na formirovanie funkcional'nyh svoystv belkovyh koncentratov / D. N. Volodin, V. K. Topalov, I. K. Kulikova [i dr.] // Molochnaya promyshlennost'. 2024. № 6. S. 48–53. https://elibrary.ru/ihvtey Zhang, F. Analysis of alphalactalbumin and betalactoglobulin from the rehydration of bovine colostrum powder using cloud point extraction and mass spectrometry / F. Zhang [et al.] // Journal of analytical methods in chemistry. 2012. 816180. https://doi.org/10.1155/2012/816180 Zhang, F. Analysis of alphalactalbumin and betalactoglobulin from the rehydration of bovine colostrum powder using cloud point extraction and mass spectrometry / F. Zhang [et al.] // Journal of analytical methods in chemistry. 2012. 816180. https://doi.org/10.1155/2012/816180 Sawyer, L. β-Lactoglobulin / L. Sawyer // Advanced Dairy Chemistry. 2013. Vol. 1 A, 2013. P. 211–259 https://doi.org/10.1007/978-1-4614-4714-6_7 Sawyer, L. β-Lactoglobulin / L. Sawyer // Advanced Dairy Chemistry. 2013. Vol. 1 A, 2013. P. 211–259 https://doi.org/10.1007/978-1-4614-4714-6_7 Goulding, D. A. Milk proteins: An overview // Milk Proteins (Third Edition) / D. A. Goulding, P. F. Fox, J. A. O’Mahony. – Academic Press, 2020. – P. 21–98. https://doi.org/10.1016/b978-0-12-815251-5.00002-5 Goulding, D. A. Milk proteins: An overview // Milk Proteins (Third Edition) / D. A. Goulding, P. F. Fox, J. A. O’Mahony. – Academic Press, 2020. – P. 21–98. https://doi.org/10.1016/b978-0-12-815251-5.00002-5 Deeth, H. Whey Proteins: An Overview // Whey Proteins: From Milk to Medicine / H. Deeth, N. Bansal, N. – Academic Press, 2018. – P. 1–50. https://doi.org/10.1016/b978-0-12-812124-5.00001-1 Deeth, H. Whey Proteins: An Overview // Whey Proteins: From Milk to Medicine / H. Deeth, N. Bansal, N. – Academic Press, 2018. – P. 1–50. https://doi.org/10.1016/b978-0-12-812124-5.00001-1 Stănciuc, N. An overview of bovine α-lactalbumin structure and functionality / N. Stănciuc, G. Râpeanu // The Annals of the University Dunarea de Jos of Galati Fascicle VI – Food Technology. 2010. Vol. 34(2). P. 82–92. Stănciuc, N. An overview of bovine α-lactalbumin structure and functionality / N. Stănciuc, G. Râpeanu // The Annals of the University Dunarea de Jos of Galati Fascicle VI – Food Technology. 2010. Vol. 34(2). P. 82–92. Korhonen, H. J. Bovine milk immunoglobulins against microbial human diseases // Dairy-Derived Ingredients: Food and Nutraceutical Uses / H. J. Korhonen, P. Marnila. – Woodhead Publishing, 2009. P. 269–289. https://doi.org/10.1533/9781845697198.2.269 Korhonen, H. J. Bovine milk immunoglobulins against microbial human diseases // Dairy-Derived Ingredients: Food and Nutraceutical Uses / H. J. Korhonen, P. Marnila. – Woodhead Publishing, 2009. P. 269–289. https://doi.org/10.1533/9781845697198.2.269 Hamarsland, H. Native whey protein with high levels of leucine results in similar post-exercise muscular anabolic responses as regular whey protein: a randomized controlled trial / H. Hamarsland [et al.] // Journal of the International Society of Sports Nutrition. 2017. Vol. 14 43. https://doi.org/10.1186/s12970-017-0202-y Hamarsland, H. Native whey protein with high levels of leucine results in similar post-exercise muscular anabolic responses as regular whey protein: a randomized controlled trial / H. Hamarsland [et al.] // Journal of the International Society of Sports Nutrition. 2017. Vol. 14 43. https://doi.org/10.1186/s12970-017-0202-y Ельчанинов, В. В. Номенклатура и биохимические свойства основных сывороточных белков. Бета-лактоглобулин / В. В. Ельчанинов // Сыроделие и маслоделие. 2009. № 2. С. 38–39. https://elibrary.ru/kzqvmp El'chaninov, V. V. Nomenklatura i biohimicheskie svoystva osnovnyh syvorotochnyh belkov. Beta-laktoglobulin / V. V. El'chaninov // Syrodelie i maslodelie. 2009. № 2. S. 38–39. https://elibrary.ru/kzqvmp Khan, S. Revealing the Dimeric Crystal and Solution Structure of β-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer–Dimer Equilibrium / S. Khan [et al.] // Biomacromolecules. 2018. Vol.19(7). P. 2905–2912. https://doi.org/10.1021/acs.biomac.8b00471 Khan, S. Revealing the Dimeric Crystal and Solution Structure of β-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer–Dimer Equilibrium / S. Khan [et al.] // Biomacromolecules. 2018. Vol.19(7). P. 2905–2912. https://doi.org/10.1021/acs.biomac.8b00471 Pike, A. C. Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase / A. C. Pike [et al.] // Structure. 1996. Vol. 4(6.) P. 691–703. https://doi.org/10.1016/s0969-2126(96)00075-5 Pike, A. C. Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase / A. C. Pike [et al.] // Structure. 1996. Vol. 4(6.) P. 691–703. https://doi.org/10.1016/s0969-2126(96)00075-5 Moore, S. A. Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution / S. A. Moore // Journal of Molecular Biology. 1997. Vol. 274(2). P. 222–236. https://doi.org/10.1006/jmbi.1997.1386 Moore, S. A. Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution / S. A. Moore // Journal of Molecular Biology. 1997. Vol. 274(2). P. 222–236. https://doi.org/10.1006/jmbi.1997.1386