EFFECT OF PROTEASES FROM STRAIN ENTEROCOCCUS FAECALIS AN1 ON LIBERATION OF ANTIMICROBIAL PEPTIDES FROM CASEINS AND THEIR STABILITY IN THE IN VITRO SIMULATED GASTROINTESTINAL SYSTEM
Abstract
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.
About the Authors
Р. МустафаеваRussian Federation
С. Гюльахмедов
Russian Federation
А. Кулиев
Russian Federation
References
1. 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.
2. 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.
3. 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.
4. 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.
5. 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.
6. Kamysu W., Okroj M., and Lukasiak J. Novel properties of antimicrobialpeptides //Acta Biochim. Pol. - 2003. - V.50, P. 236-239.
7. 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.
8. Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 // Nature. - 1970. - V.227. P. 680-685.
9. 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.
10. 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.
11. Tagg J., Dajani A., Wannamaker L. Bacteriocins of Gram-positive bacteria // Bacteriol.Rev. - 1976. - V.40. P.722-756.