geomgouГеографическая среда и живые системыGeographical Environment and Living Systems2712-76132712-7621Московский государственный областной университетgeomgou-658Research ArticleСтатьиВЛИЯНИЕ ПРОТЕАЗ ШТАММА ENTEROCOCCUS FAECALIS AN1 НА ОБРАЗОВАНИЕ АНТИМИКРОБНЫХ ПЕПТИДОВ ИЗ КАЗЕИНОВ И ИХ РЕЗИСТЕНТНОСТЬ В УСЛОВИЯХ IN VITRO СТИМУЛИРОВАННОЙ* ЖЕЛУДОЧНО-КИШЕЧНОЙ СИСТЕМЫEFFECT OF PROTEASES FROM STRAIN ENTEROCOCCUS FAECALIS AN1 ON LIBERATION OF ANTIMICROBIAL PEPTIDES FROM CASEINS AND THEIR STABILITY IN THE IN VITRO SIMULATED GASTROINTESTINAL SYSTEMМустафаеваР. С.rugiyamustafayeva@mail.ruГюльахмедовС. Г.sahib66@ rambler.ruКулиевА. А.sahib66@ rambler.ruБакинский государственный университетRussian Federation201227052022033842Copyright © Мустафаева Р.С., Гюльахмедов С.Г., Кулиев А.А., 20222022Мустафаева Р.С., Гюльахмедов С.Г., Кулиев А.А.Мустафаева Р.С., Гюльахмедов С.Г., Кулиев А.А.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.geoecosreda.ru/jour/article/view/658

Целью исследования было изучить по- тенциал протеолитического штамма Enterococcus faecalis AN1, генерировать антимикробные пептиды из казеинов, а также определить влияние последующего гидролиза пепсином и панкреатином в условиях in vitro симулиро- ванной желудочно-кишечной системы на данную актив- ность. Анализ гидролиза субстрата и образования пеп- тидов проводили при помощи SDS-ПААГ-электрофореза и ОФ ВЭЖХ. Гидролизат казеинов протеазами штам- ма проявил антимикробную активность против Listeria monocytogenes EGDe107776. Антимикробная активность в гидролизате сохранялась после гидролиза пепсином, однако при воздействии панкреатина полностью исче- зала. Более того, предварительный гидролиз казеинов протеазами штамма Enterococcus faecalis AN1 улучшал их переваривание пепсином. Исследуемый штамм об- ладает потенциалом в производстве функциональных молочных продуктов.

The aim of the present research was to study the effect of proteolytic strain Enterococcus faecalis AN1 on liberation of casein-derived antimicrobial peptides, as well as also to determine the infl uence of the subsequent hydrolysis by pepsin and pancreatin in the in vitro stimulated gastrointestinal system on this activity. The protein hydrolysis and peptide production were analyzed with the help of SDS PAGE and RP-HPLC. The peptides released upon hydrolysis of caseins with the studied strain presented antimicrobial activity against Listeria monocytogenes EGDe107776. Antimicrobial activity of casein-derived peptides was stable after pepsin hydrolysis; however, the effect totally disappeared after pancreatic digestion. Moreover, prehydrolysis of caseins by proteases from strain Enterococcus faecalis AN1 increased their digestion by pepsin. The strain under study could be a potential starter for production of functional dairy products.

протеазыказеиныантимикробные пептидыproteasescaseinsantimicrobial peptidesReferencesAhmadova A., Abdullayeva N.A., Quseynova N.F., Quliyev A.A. Milk caseins hydrolysis by strain Enterococcus faecalis AN1 //Proceedings of the Azerbaijan National Academy of Sciences. - 2010. - № 6. - P. 25-85.Ahmadova A., Abdullayeva N.A., Quseynova N.F., Quliyev A.A. Milk caseins hydrolysis by strain Enterococcus faecalis AN1 //Proceedings of the Azerbaijan National Academy of Sciences. - 2010. - № 6. - P. 25-85.Centeno J.A., Menendez S., Hermida M., Rodriguez- Otero J.L. Eff ect of the addition of Enterococcus faecalis in Cebreiro cheese manufacture.// International Journal of Food Microbiology. - 1999. - V. 48. - P. 97-111.Centeno J.A., Menendez S., Hermida M., Rodriguez- Otero J.L. Eff ect of the addition of Enterococcus faecalis in Cebreiro cheese manufacture.// International Journal of Food Microbiology. - 1999. - V. 48. - P. 97-111.Exterkate F., Alting A., Bruinenberg P. Diversity of cell envelope proteinase specifi city among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.// Applied and Environmental Microbiology. 1993. - V.59. - P. 3640-3647.Exterkate F., Alting A., Bruinenberg P. Diversity of cell envelope proteinase specifi city among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.// Applied and Environmental Microbiology. 1993. - V.59. - P. 3640-3647.Fira D., Kojic M., Banina A. et al. Characterization of cell envelope-associated proteinases of thermophilic lactobacilli // J.Appl.Microbiol. 2001. - V. 90. - P. 123-130.Fira D., Kojic M., Banina A. et al. Characterization of cell envelope-associated proteinases of thermophilic lactobacilli // J.Appl.Microbiol. 2001. - V. 90. - P. 123-130.Gobbetti M., Stepaniak L., De Angelis M., Corsetti A. and Di Cagno R. Latent bioactive peptides in milk proteins: proteolytic activation and signifi cance in dairy processing. // Crit. Rev. Food Sci. Nutr. - 2002. V. 42. P. 223-239.Gobbetti M., Stepaniak L., De Angelis M., Corsetti A. and Di Cagno R. Latent bioactive peptides in milk proteins: proteolytic activation and signifi cance in dairy processing. // Crit. Rev. Food Sci. Nutr. - 2002. V. 42. P. 223-239.Kamysu W., Okroj M., and Lukasiak J. Novel properties of antimicrobialpeptides //Acta Biochim. Pol. - 2003. - V.50, P. 236-239.Kamysu W., Okroj M., and Lukasiak J. Novel properties of antimicrobialpeptides //Acta Biochim. Pol. - 2003. - V.50, P. 236-239.Kunji E.R.S., Mierau I., Hagfi ng A., Poolman B.I., Konings W.N. Th e proteolytic systems of lactic acid bacteria // Antonie van Leeuwenhoek. - 1996. - V.70, P.187-221.Kunji E.R.S., Mierau I., Hagfi ng A., Poolman B.I., Konings W.N. Th e proteolytic systems of lactic acid bacteria // Antonie van Leeuwenhoek. - 1996. - V.70, P.187-221.Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 // Nature. - 1970. - V.227. P. 680-685.Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 // Nature. - 1970. - V.227. P. 680-685.Lahov E., and Regelson W.. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem.Toxicol. - 1996. V.34. P.131-145.Lahov E., and Regelson W.. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem.Toxicol. - 1996. V.34. P.131-145.Mouecoucou J., Villaume C., Sanchez C., Mejean L. β-Lactoglobulin/ polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of diff erent molecular weight cut-off s.// Biochim.Biophys.Acta, 22.01.2004. - V.1670. - is.2. P.105-112.Mouecoucou J., Villaume C., Sanchez C., Mejean L. β-Lactoglobulin/ polysaccharide interactions during in vitro gastric and pancreatic hydrolysis assessed in dialysis bags of diff erent molecular weight cut-off s.// Biochim.Biophys.Acta, 22.01.2004. - V.1670. - is.2. P.105-112.Tagg J., Dajani A., Wannamaker L. Bacteriocins of Gram-positive bacteria // Bacteriol.Rev. - 1976. - V.40. P.722-756.Tagg J., Dajani A., Wannamaker L. Bacteriocins of Gram-positive bacteria // Bacteriol.Rev. - 1976. - V.40. P.722-756.

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