Moscow, Россия
Yekaterinburg, Россия
Yekaterinburg, Россия
Yekaterinburg, Россия
Yekaterinburg, Россия
Peptides of plant and animal origin have good anti-diabetic prospects. The research objective was to use bovine colostrum peptides to reduce hyperglycemia in diabetic rats. Bovine colostrum peptides were obtained by trypsin hydrolysis of colostrum proteins with preliminary extraction of triglycerides. The study involved four groups of Wistar rats with seven animals per group. Group 1 served as control; group 2 received 300 mg/kg of trypsin hydrolysate of bovine colostrum as part of their daily diet for 30 days. Groups 3 and 4 had diabetes mellitus caused by intraperitoneal injections of 110 mg/kg of nicotinamide and 65 mg/kg of streptozotocin. Group 4 also received 300 mg/kg trypsin hydrolysate of bovine colostrum intragastrically five times a week for 30 days. Three peptides were isolated from the trypsin hydrolysate of bovine colostrum and tested for the sequence of amino acids and molecular weight. Their identification involved the Protein NCBI database, followed by 2D and 3D modeling, which revealed their chemical profile, pharmacological properties, and antioxidant activity. The diabetic rats treated with colostrum peptides had lower glucose, glycated hemoglobin, malondialdehyde, and catalase activity but a higher content of glutathione in the blood. Their leukocytes and erythrocytes also demonstrated less deviation from the standard. The antioxidant effect of colostrum protein hydrolysate depended on a peptide with the amino acid sequence of SQKKKNCPNGTRIRVPGPGP and a mass of 8.4 kDa. Colostrum peptides reduced hyperglycemia and oxidative stress in diabetic rats. The research revealed good prospects for isolating individual colostrum peptides to be tested for antidiabetic properties.
Peptides, bovine colostrum, diabetes mellitus, glucose, glycated hemoglobin, antioxidant activity
1. International Diabetes Federation: Diabetes Atlas 8th edition. 2017.
2. Ademosun AO. Glycemic properties of soursop-based ice cream enriched with moringa leaf powder. Foods and Raw Materials. 2021;9(2):207-214. https://doi.org/10.21603/2308-4057-2021-2-207-214
3. Zaytseva LV, Ruban NV, Tsyganova TB, Mazukabzova EV. Fortified confectionery creams on vegetable oils with a modified carbohydrate profile. Food Processing: Techniques and Technology. 2022;52(3):500-510. (In Russ.). https://doi.org/10.21603/2074-9414-2022-3-2377
4. Artasensi A, Pedretti A, Vistoli G, Fumagalli L. Type 2 diabetes mellitus: A review of multi-target drugs. Molecules. 2020;25(8). https://doi.org/10.3390/molecules25081987
5. Holst JJ. From the incretin concept and the discovery of GLP-1 to today's diabetes therapy. Frontiers in Endocrinology. 2019;10. https://doi.org/10.3389/fendo.2019.00260
6. Pereira ASP, Banegas-Luna AJ, Peña-García J, Pérez-Sánchez H, Apostolides Z. Evaluation of the anti-diabetic activity of some common herbs and spices: Providing new insights with inverse virtual screening. Molecules. 2019;24(22). https://doi.org/10.3390/molecules24224030
7. Lin Y-H, Chen G-W, Yeh CH, Song H, Tsai J-S. Purification and identification of angiotensin I-converting enzyme inhibitory peptides and the antihypertensive effect of Chlorella sorokiniana protein hydrolysates. Nutrients. 2018;10(10). https://doi.org/10.3390/nu10101397
8. Andreeva A, Budenkova E, Babich O, Sukhikh S, Ulrikh E, Ivanova S, et al. Production, purification, and study of the amino acid composition of microalgae proteins. Molecules. 2021;26(9). https://doi.org/10.3390/molecules26092767
9. Li Y, Aiello G, Bollati C, Bartolomei M, Arnoldi A, Lammi C. Phycobiliproteins from Arthrospira platensis (spirulina): A new source of peptides with dipeptidyl peptidase-IV inhibitory activity. Nutrients. 2020;12(3). https://doi.org/10.3390/nu12030794
10. Novoselova MV, Prosekov AYu. Technological options for the production of lactoferrin. Foods and Raw Materials. 2016;4(1):90-101. https://doi.org/10.21179/2308-4057-2016-1-90-101
11. Manzanares P, Gandía M, Garrigues S, Marcos JF. Improving health-promoting effects of food-derived bioactive peptides through rational design and oral delivery strategies. Nutrients. 2019;11(10). https://doi.org/10.3390/nu11102545
12. Suo S-K, Zheng S-L, Chi C-F, Luo H-Y, Wang B. Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts-milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells. Frontiers in Nutrition. 2022;9. https://doi.org/10.3389/fnut.2022.957778
13. Ryazantseva KA, Agarkova EYu, Fedotova OB. Continuous hydrolysis of milk proteins in membrane reactors of various configurations. Foods and Raw Materials. 2021;9(2):271-281. https://doi.org/10.21603/2308-4057-2021-2-271-281.
14. Ayala-Niño A, Rodríguez-Serrano GM, González-Olivares LG, Contreras-López E, Regal-López P, Cepeda-Saez A. Sequence identification of bioactive peptides from amaranth seed proteins (Amaranthus hypochondriacus spp.). Molecules. 2019;24(17). https://doi.org/10.3390/molecules24173033
15. Rubak YuT, Nuraida L, Iswantini D, Prangdimurti E. Angiotensin-I-converting enzyme inhibitory peptides in milk fermented by indigenous lactic acid bacteria. Veterinary World. 2020;13(2):345-353. https://doi.org/10.14202/vetworld.2020.345-353
16. Zhang R, Chen J, Mao X, Qi P, Zhang X. Separation and lipid inhibition effects of a novel decapeptide from Chlorella pyenoidose. Molecules. 2019;24(19). https://doi.org/10.3390/molecules24193527
17. Valenzuela Zamudio F, Segura Campos MR. Amaranth, quinoa and chia bioactive peptides: a comprehensive review on three ancient grains and their potential role in management and prevention of Type 2 diabetes. Critical Reviews in Food Science and Nutrition. 2020;62(10):2707-2721. https://doi.org/10.1080/10408398.2020.1857683
18. Quintero-Soto MF, Chávez-Ontiveros J, Garzón-Tiznado JA, Salazar-Salas NY, Pineda-Hidalgo KV, Delgado-Vargas F, et al. Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates. Journal of Food Science. 2021;86(7):2962-2977. https://doi.org/10.1111/1750-3841.15778
19. Uyama T, Kelton DF, Winder CB, Dunn J, Goetz HM, LeBlanc SJ, et al. Colostrum management practices that improve the transfer of passive immunity in neonatal dairy calves: A scoping review. PLoS ONE. 2022;17(6). https://doi.org/10.1371/journal.pone.0269824
20. Tikhonov SL, Tikhonova NV, Tursunov KhKh, Danilova IG, Lazarev VA. Peptides of trypsin hydrolyzate in bovine colostrum. Food Processing: Techniques and Technology. 2023;53(1):150-158. (In Russ.). https://doi.org/10.21603/2074-9414-2023-1-2422
21. Playford RJ, Weiser MJ. Bovine colostrum: Its constituents and uses. Nutrients. 2021;13(1). https://doi.org/10.3390/nu13010265
22. Brenmoehl J, Ohde D, Wirthgen E, Hoeflich A. Cytokines in milk and the role of TGF-beta. Best Practice and Research Clinical Endocrinology and Metabolism. 2018;32(1):47-56. https://doi.org/10.1016/j.beem.2018.01.006
23. Inabu Y, Pyo J, Pletts S, Guan LL, Steele MA, Sugino T. Effect of extended colostrum feeding on plasma glucagon-like peptide-1 concentration in newborn calves. Journal of Dairy Science. 2019;102(5):4619-4627. https://doi.org/10.3168/jds.2018-15616
24. Ashok NR, Aparna HS. Empirical and bioinformatic characterization of buffalo (Bubalus bubalis) colostrum whey peptides & their angiotensin I-converting enzyme inhibition. Food Chemistry. 2017;228:582-594. https://doi.org/10.1016/j.foodchem.2017.02.032
25. Agarkova EYu, Ryazantseva KA, Kruchinin AG. Anti-diabetic activity of whey proteins. Food Processing: Techniques and Technology. 2020;50(2):306-318. (In Russ.). https://doi.org/10.21603/2074-9414-2020-2-306-318
26. Golovach TN, Kurchenko VP, Tarun EI. Protein-peptide composition and radical reducing properties of fermented bovine colostrum. Food Industry: Science and Technologies. 2016;33(3):57-63. (In Russ.). https://elibrary.ru/XAMKJF
27. Feduraev P, Skrypnik L, Nebreeva S, Dzhobadze G, Vatagina A, Kalinina E, et al. Variability of phenolic compound accumulation and antioxidant activity in wild plants of some Rumex species (Polygonaceae). Antioxidants. 2022;11(2). https://doi.org/10.3390/antiox11020311
28. Spasov AA, Vorohkova MP, Snegur GL, Cheplyaeva NI, Chepurnova MV. Experimental model of a type 2 diabetes. Journal Biomed. 2011;(3):12-18. (In Russ.). https://elibrary.ru/OJBTOH
29. Stalʹnaya ID, Garishvili TG. Determining malondialdehyde with thiobarbituric acid. In: Orekhovicha VN, editor. Modern methods in biochemistry. Moscow: Meditsina; 1977. pp. 66-68. (In Russ.).
30. Verevkina IV, Tochilkin AI, Popova NA. Colorimetric determination of SH-groups and -SS-bonds in proteins with 5,5'-dithiobis(2-nitrobenzoic) acid. In: Orekhovicha VN, editor. Modern methods in biochemistry. Moscow: Meditsina; 1977. pp. 223-231. (In Russ.).
31. Korolyuk MA, Ivanova LN, Mayorova IG, Tokarev VE. Determining catalase activity. Laboratory Sphere. 1988;(4):44-47. (In Russ.).
32. Sonklin C, Laohakunjit N, Kerdchoechuen O. Assessment of antioxidant properties of membrane ultrafiltration peptides from mungbean meal protein hydrolysates. PeerJ. 2018;6. https://doi.org/10.7717/peerj.5337
33. Meza-Espinoza L, Sáyago-Ayerdi SG, García-Magaña ML, Tovar-Pérez EG, Yahia EM, Vallejo-Cordoba B, et al. Antioxidant capacity of egg, milk and soy protein hydrolysates and biopeptides produced by Bromelia pinguin and Bromelia karatas-derived proteases. Emirates Journal of Food and Agriculture. 2018;30(2):122-130. https://doi.org/10.9755/ejfa.2018.v30.i2.1604
34. Samaranayaka AGP, Li-Chan ECY. Food-derived peptidic antioxidants: A review of their production, assessment, and potential applications. Journal of Functional Foods. 2011;3(4):229-254. https://doi.org/10.1016/j.jff.2011.05.006
35. Carrasco-Castilla J, Hernández-Álvarez AJ, Jiménez-Martínez C, Jacinto-Hernández C, Alaiz M, Girón-Calle J, et al. Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates. Food Chemistry. 2012;131(4):1157-1164. https://doi.org/10.1016/j.foodchem.2011.09.084
36. Wang Y-Y, Wang C-Y, Wang S-T, Li Y-Q, Mo H-Z, He J-X. Physicochemical properties and antioxidant activities of tree peony (Paeonia suffruticosa Andr.) seed protein hydrolysates obtained with different proteases. Food Chemistry. 2021;345. https://doi.org/10.1016/j.foodchem.2020.128765
37. Queiroz LAD, Assis JB, Guimarães JPT, Sousa ESA, Milhomem AC, Sunahara KKS, et al. Endangered lymphocytes: The effects of alloxan and streptozotocin on immune cells in type 1 induced diabetes. Mediators Inflammation. 2021;2021. https://doi.org/10.1155/2021/9940009
