Obtaining and characteristic of degradation products of Lactobacillus acidophilus K 3111 peptidoglycan
It is shown in the article that low molecular weight degradation products of peptidoglycans of bacterial walls possess high immunotropic activity and can stimulate evolutionarily fixed mechanisms of immune response. It is proposed to obtain low molecular weight fragments of peptidoglycans of cell walls of Lactobacillus acidophilus K 3111 – muropeptides. Fragmentation was carried out by combining physical and enzymatic methods of disintegration. As a physical factor of influence, an ultrasonic treatment was used, as enzymatic factor, a treatment with proteases of digestive, plant and microbial origin was used. These enzymes have a significant range of substrate specificity and can catalyze the specific binding of peptidoglycans to bacterial walls. The regularities of ultrasonic disintegration of Lactobacillus acidophilus K 311 has been investigated in the article. The rational conditions of ultrasonic disintegration are the treatment of biomass at a frequency of 35 kHz for 600 seconds. Under these conditions, the maximum amount of amino acids is accumulated in the disintegrate and the integrity of most bacterial cells is violated. The regularities of the enzymolysis of peptidoglycans of cell walls of Lactobacillus acidophilus K 3111 by pancreatin, papain and protosubtilin has been determined. It has been shown that ultrasonic disintegration, which precedes enzymatic hydrolysis, contributes to a significant increase in the content of low molecular weight peptides in hydrolysates by almost 50%. The expediency of using an enzyme of plant origin papain for enzymatic fragmentation of peptidoglycan is substantiated. When the ratio of the enzyme (papain): substrate 1: 200 and the duration of the process for 180 minutes, the highest content of low molecular weight peptides in hydrolysates (6.6 mg/cm3) is achieved. It is proved that the target compounds muropeptides are contained in the products of enzymatic hydrolysis, the content of muropeptides reaches 38% of the total amount of low molecular weight peptides at the hydrolysis by papain, 31% –by pancreatin and 23% – by protosubtilin.
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