Determination of the enzyme destruction rational mode of biomass autolysate of lactic acid bacteria
Keywords:biomass, lactic acid bacteria, autolysate, enzymatic hydrolysis, pancreatin, peptidoglycan, muramyl peptide, immunotropic properties, mathematical modeling
It is shown that the degradation products of peptidoglycans of lactic acid bacteria cell walls that are related to the muramyl peptide series compounds are promising components of food ingredients and dietary supplements for the nutritional support of the population suffering from disorders of the immune system.
The expediency of autolysis of lactic acid bacteria biomass to increase the enzymatic degradation efficiency of peptidoglycans of their cell walls has been proven. The accumulation of low molecular weight peptides in the enzymatic hydrolysis of biomass under rational parameters, which was not subjected to autolysis, is 0.260 mg/cm3, in the enzymatic hydrolysis of biomass that was subjected to autolysis is 0.569 mg/cm3. Rational regimes of enzymatic hydrolysis of the composition of lactic acid bacteria (enzyme concentration of 12.5 mg/cm3, substrate concentration of 70.0 mg/cm3, duration of enzymatic hydrolysis of 245.6 min) were determined using mathematical planning methods of multifactorial experiments, which made it possible to significantly optimize and improve the work efficiency.The affiliation of low molecular weight peptides obtained under the rational conditions of enzymatic hydrolysis to immunological compounds of the muramyl peptide series has been proven by gel chromatography and IR spectroscopy methods. It is determined that the molecular weight of the obtained low molecular weight peptides is in the range of 294 – 650 Da, which, in fact, corresponds to the molecular weight of muramyl dipeptide and glucosaminylmuramyl dipeptide. In the IR spectrum of low molecular weight peptides, the absorption bands are noted, which correspond to fluctuations of free amino groups, peptide bonds, which, in fact, occur in the structure of peptides, pyranose glucose forms that are part of muramic acid and N-acetylglucosamine of peptidoglycan, muramyl dipeptide and glucosaminylmuramyl dipeptide. Also, fluctuations of β-glycoside bonds, which binds the remains of muramic acid and N-acetylglucosamine in peptidoglycan and glucosaminylmuramyl dipeptide are marked in the IR spectrum of low molecular weight peptides
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Copyright (c) 2018 Antonina Kapustian, Natalia Cherno, Georgii Stankevich, Iryna Kolomiiets, Oksana Matsjuk, Lubov Musiy, Iryna Slyvka
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