nogrЭкспериментальная и клиническая гастроэнтерологияExperimental and Clinical Gastroenterology1682-8658«Global Media Technologies»10.31146/1682-8658-ecg-207-11-177-182nogr-2205Research ArticleЭКСПЕРИМЕНТАЛЬНАЯ ГАСТРОЭНТЕРОЛОГИЯEXPERIMENTAL GASTROENTEROLOGYВлияние гидролизатов казеина, полученных под воздействием желудочного и поджелудочного сока, на липидемические показатели кровиThe effect of casein hydrolysates, incurred due to the high risk of cardiac and pancreatic juice, on blood lipid parametersДжалаловаО. К.DjalalovaO. K.djalalova.ozoda@gmail.comАндижанский государственный медицинский институтРоссияAndijan State Medical InstituteRussian Federation202223012023011177182Copyright © Джалалова О.К., 20232023Джалалова О.К.Djalalova O.K.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.nogr.org/jour/article/view/2205

При изучении влияния кормления эмульсии из желатина, подвергнутого инкубации с желудочным соком, и подсолнечного масла, на показатели триглицеридов и холестерина крови по сравнению со средними показателями до кормления были выше, а после кормления были незначительно выше в сопоставлении с эмульсией желатина и подсолнечного масла. При этом показатели триглицеридов и холестерина недостоверно выше на протяжении всего 6 часового периода наблюдения по сравнению с показателями до кормления. Также выявлено, что средние показатели прироста триглицеридов и холестерина под влиянием кормления эмульсией из желатина и подсолнечного масла, подвергнутого инкубации с желудочным соком не существенно выше, а с поджелудочным соком не значительно ниже таковых после кормления эмульсией из желатина и подсолнечного масла. Это указывает на то, что гидролизаты желатина, полученные под влиянием, как желудочного, так и поджелудочного сока, существенно не влияют на переваривание и всасывание жиров в тонком кишечнике.

When studying the effect of feeding, emulsions of gelatin subjected to incubation with gastric juice and sunflower oil on triglycerides and blood cholesterol were higher compared to the average values before feeding, and after feeding were slightly higher compared to the emulsion of gelatin and sunflower oil. At the same time, triglyceride and cholesterol values were not significantly higher throughout the entire 6-hour observation period compared to pre-feeding values. It was also found that the average increase in triglycerides and cholesterol under the influence of feeding with an emulsion of gelatin and sunflower oil incubated with gastric juice is not significantly higher, and with pancreatic juice is not significantly lower than those after feeding with an emulsion of gelatin and sunflower oil. This indicates that gelatin hydrolysates obtained under the influence of both gastric and pancreatic juice do not significantly affect the digestion and absorption of fats in the small intestine.

триглицеридхолестеринжелатинподсолнечное масложелудочный и поджелудочный сокtriglyceridecholesterolgelatinsunflower oilgastric and pancreatic juiceReferencesAl-Shamsi K.A., Mudgil P., Hassan H. M., Maqsood S. Camel milk protein hydrolysates with improved technofunctional properties and enhanced antioxidant potential in in vitro and in food model systems. J Dairy Sci. 2018 Jan;101(1):47-60. doi: 10.3168/jds.2017-13194.Al-Shamsi K.A., Mudgil P., Hassan H. M., Maqsood S. Camel milk protein hydrolysates with improved technofunctional properties and enhanced antioxidant potential in in vitro and in food model systems. J Dairy Sci. 2018 Jan;101(1):47-60. doi: 10.3168/jds.2017-13194.Arihara K. Strategies for designing novel functional meat products. Meat Sci. 2006 Sep;74(1):219-29. doi: 10.1016/j.meatsci.2006.04.028.Arihara K. Strategies for designing novel functional meat products. Meat Sci. 2006 Sep;74(1):219-29. doi: 10.1016/j.meatsci.2006.04.028.Cheung I.W., Nakayama S., Hsu M. N., Samaranayaka A. G., Li-Chan E. C. Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. J Agric Food Chem. 2009 Oct 14;57(19):9234-42. doi: 10.1021/jf9018245.Cheung I.W., Nakayama S., Hsu M. N., Samaranayaka A. G., Li-Chan E. C. Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. J Agric Food Chem. 2009 Oct 14;57(19):9234-42. doi: 10.1021/jf9018245.Deming T. J. Polypeptide hydrogels via a unique assembly mechanism. Soft Matter. 2005 May 27;1(1):28-35. doi: 10.1039/b500307e.Deming T. J. Polypeptide hydrogels via a unique assembly mechanism. Soft Matter. 2005 May 27;1(1):28-35. doi: 10.1039/b500307e.Doll T.A, Raman S., Dey R., Burkhard P. Nanoscale assemblies and their biomedical applications. J R Soc Interface. 2013 Jan 9;10(80):20120740. doi: 10.1098/rsif.2012.0740.Doll T.A, Raman S., Dey R., Burkhard P. Nanoscale assemblies and their biomedical applications. J R Soc Interface. 2013 Jan 9;10(80):20120740. doi: 10.1098/rsif.2012.0740.Erdmann K., Cheung B. W., Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem. 2008 Oct;19(10):643-54. doi: 10.1016/j.jnutbio.2007.11.010.Erdmann K., Cheung B. W., Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem. 2008 Oct;19(10):643-54. doi: 10.1016/j.jnutbio.2007.11.010.Friedman M. Nutritional value of proteins from different food sources: A review. J. Agric. Food Chem. 1996; 44: 6-29.Friedman M. Nutritional value of proteins from different food sources: A review. J. Agric. Food Chem. 1996; 44: 6-29.Hall F.G., Jones O. G., O’Haire M.E., Liceaga A. M. Functional properties of tropical banded cricket (Gryllodes sigillatus) protein hydrolysates. Food Chem. 2017 Jun 1;224:414-422. doi: 10.1016/j.foodchem.2016.11.138.Hall F.G., Jones O. G., O’Haire M.E., Liceaga A. M. Functional properties of tropical banded cricket (Gryllodes sigillatus) protein hydrolysates. Food Chem. 2017 Jun 1;224:414-422. doi: 10.1016/j.foodchem.2016.11.138.Howard A., Udenigwe C. C. Mechanisms and prospects of food protein hydrolysates and peptide-induced hypolipidaemia. Food Funct. 2013 Jan;4(1):40-51. doi: 10.1039/c2fo30216k.Howard A., Udenigwe C. C. Mechanisms and prospects of food protein hydrolysates and peptide-induced hypolipidaemia. Food Funct. 2013 Jan;4(1):40-51. doi: 10.1039/c2fo30216k.Ju-Hwan O., Lee Y. S. Hypolipidemic effects of peptide fractions of casein on serum lipids in rats fed normal or high fat diet. Journal-korean society of food science and nutrition. 2002;31(2):263-270.Ju-Hwan O., Lee Y. S. Hypolipidemic effects of peptide fractions of casein on serum lipids in rats fed normal or high fat diet. Journal-korean society of food science and nutrition. 2002;31(2):263-270.Kim E., Lee S., Jeon B., Moon S., Kim B., Park T., Han J., Park P. Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein. Food chemistry. 114;(4):1365-1370. doi: 10.1016/j.foodchem.2008.11.035.Kim E., Lee S., Jeon B., Moon S., Kim B., Park T., Han J., Park P. Purification and characterisation of antioxidative peptides from enzymatic hydrolysates of venison protein. Food chemistry. 114;(4):1365-1370. doi: 10.1016/j.foodchem.2008.11.035.Korhonen H., Pihlanto A. Bioactive peptides: Production and functionality.Int. Dairy J. 2006;16:945-960.Korhonen H., Pihlanto A. Bioactive peptides: Production and functionality.Int. Dairy J. 2006;16:945-960.Lam R.S., Nickerson M. T. Food proteins: a review on their emulsifying properties using a structure-function approach. Food Chem. 2013 Nov 15;141(2):975-84. doi: 10.1016/j.foodchem.2013.04.038.Lam R.S., Nickerson M. T. Food proteins: a review on their emulsifying properties using a structure-function approach. Food Chem. 2013 Nov 15;141(2):975-84. doi: 10.1016/j.foodchem.2013.04.038.Majumder K., Wu J. Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs. J Agric Food Chem. 2009 Jan 28;57(2):471-7. doi: 10.1021/jf8028557.Majumder K., Wu J. Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs. J Agric Food Chem. 2009 Jan 28;57(2):471-7. doi: 10.1021/jf8028557.Mandal D, Nasrolahi Shirazi A, Parang K. Self-assembly of peptides to nanostructures. Org Biomol Chem. 2014 Jun 14;12(22):3544-61. doi: 10.1039/c4ob00447g.Mandal D, Nasrolahi Shirazi A, Parang K. Self-assembly of peptides to nanostructures. Org Biomol Chem. 2014 Jun 14;12(22):3544-61. doi: 10.1039/c4ob00447g.Matsui T., Matsumoto K. Antihypertensive peptides from natural resources. Advances in Phytomedicine. 2006;(2):255-271. doi: 10.1016/S1572-557X(05)02015-5.Matsui T., Matsumoto K. Antihypertensive peptides from natural resources. Advances in Phytomedicine. 2006;(2):255-271. doi: 10.1016/S1572-557X(05)02015-5.Qi M., Hettiarachchy N. S., Kalapathy U. Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science. 1997;62(6):1110-1115.Qi M., Hettiarachchy N. S., Kalapathy U. Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science. 1997;62(6):1110-1115.Ryan J.T., Ross R. P., Bolton D., Fitzgerald G. F., Stanton C. Bioactive peptides from muscle sources: meat and fish. Nutrients. 2011 Sep;3(9):765-91. doi: 10.3390/nu3090765.Ryan J.T., Ross R. P., Bolton D., Fitzgerald G. F., Stanton C. Bioactive peptides from muscle sources: meat and fish. Nutrients. 2011 Sep;3(9):765-91. doi: 10.3390/nu3090765.Tsumura K. Improvement of the physicochemical properties of soybean proteins by enzymatic hydrolysis. Food Science and Technology Research. 2009;15(4):381-388.Tsumura K. Improvement of the physicochemical properties of soybean proteins by enzymatic hydrolysis. Food Science and Technology Research. 2009;15(4):381-388.Vercruysse L., Van Camp J., Smagghe G. ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review. J Agric Food Chem. 2005 Oct 19;53(21):8106-15. doi: 10.1021/jf0508908.Vercruysse L., Van Camp J., Smagghe G. ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review. J Agric Food Chem. 2005 Oct 19;53(21):8106-15. doi: 10.1021/jf0508908.Vermeirssen V, Van Camp J, Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr. 2004 Sep;92(3):357-66. doi: 10.1079/bjn20041189.Vermeirssen V, Van Camp J, Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr. 2004 Sep;92(3):357-66. doi: 10.1079/bjn20041189.

The authors declare that there are no conflicts of interest present.