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The possibility of muropeptides obtaining of peptidoglycans of Lactobacillus delbrueckii subsp. Bulgaricus B-3964 cell walls by the combination of the use of autolytic processes and enzyme treatment of biomass with the participation of lysozyme and papain has been considered. It has been established that the most significant autolytic changes in biomass occur in the application of high-temperature processing (90°C for 30 minutes) in the final stage of the logarithmic phase of bacterial growth. Thus, after eighth hour of biomass incubation at 37°C, the amino acid content in the culture medium was 1.8 mg/cm3, and at 90°C it was 5.7 mg/cm3. In order to further destruction of biomass autolysate and obtaining of low molecular weight peptidoglycan fragments, the process of its enzymatic hydrolysis was studied with lysozyme and papain separately and at their combination. The highest content of low molecular weight peptides in the reaction medium occurred at enzymatic hydrolysis of biomass Lactobacillus delbrueckii subsp. Bulgaricus B-3964 by the composition of enzymes at a ratio of lysozyme : papain 1:2. At a concentration of enzymes 10 mg/cm3, the content of low molecular weight peptides was 7.2 mg/cm3 after eighth hour of incubation of the reaction mixture. The results of studies have been shown that the efficiency of enzymatic hydrolysis of autolysates is much higher. Thus, the amount of low molecular weight peptides in the hydrolysate obtained by processing the autolysate with the composition of lysozyme : papain 1:2 at an enzymes concentration 10 mg/cm3 and the duration of the process for 8 hours by 36% higher than for similar hydrolysis parameters without the use of the process of autolysis.The method of gel chromatography was proved that in the hydrolysate there are fractions of protein compounds with a molecular weight in the range of 70–90 kDa, 30–40 kDa and 294–650 Da. The molecular weight of the latter fraction corresponds to the mass of the muramyl dipeptide. The presence of muropeptides was proved by reaction with the Anthron reagent.
The possibility of muropeptides obtaining of peptidoglycans of Lactobacillus delbrueckii subsp. Bulgaricus B-3964 cell walls by the combination of the use of autolytic processes and enzyme treatment of biomass with the participation of lysozyme and papain has been considered. It has been established that the most significant autolytic changes in biomass occur in the application of high-temperature processing (90°C for 30 minutes) in the final stage of the logarithmic phase of bacterial growth. Thus, after eighth hour of biomass incubation at 37°C, the amino acid content in the culture medium was 1.8 mg/cm3, and at 90°C it was 5.7 mg/cm3. In order to further destruction of biomass autolysate and obtaining of low molecular weight peptidoglycan fragments, the process of its enzymatic hydrolysis was studied with lysozyme and papain separately and at their combination. The highest content of low molecular weight peptides in the reaction medium occurred at enzymatic hydrolysis of biomass Lactobacillus delbrueckii subsp. Bulgaricus B-3964 by the composition of enzymes at a ratio of lysozyme : papain 1:2. At a concentration of enzymes 10 mg/cm3, the content of low molecular weight peptides was 7.2 mg/cm3 after eighth hour of incubation of the reaction mixture. The results of studies have been shown that the efficiency of enzymatic hydrolysis of autolysates is much higher. Thus, the amount of low molecular weight peptides in the hydrolysate obtained by processing the autolysate with the composition of lysozyme : papain 1:2 at an enzymes concentration 10 mg/cm3 and the duration of the process for 8 hours by 36% higher than for similar hydrolysis parameters without the use of the process of autolysis.The method of gel chromatography was proved that in the hydrolysate there are fractions of protein compounds with a molecular weight in the range of 70–90 kDa, 30–40 kDa and 294–650 Da. The molecular weight of the latter fraction corresponds to the mass of the muramyl dipeptide. The presence of muropeptides was proved by reaction with the Anthron reagent.
The possibility of obtaining bioavailable mixed ligand chelate complexes of calcium has been considered. As bioligands, it is proposed to use the metabolic products of probiotic bacteria combination and products of enzymatic hydrolysis of peptidoglycans of their cell walls. The culture fluid of probiotic bacteria composition has been investigated for the determination of metabolites in its composition that can participate in the formation of calcium chelate complexes. The qualitative composition and quantitative content of organic acids of a culture fluid have been determined. It has been established that it contains the following acids: oxalic (1.6 mg/dm3), citric (22.1 mg/dm3), acetic (575.8 mg/dm3), lactic (236.3 mg/dm3), benzoic (1.5 mg/dm3). In addition, it has been found that in the composition of the culture liquid, free amino acids and soluble protein are also present in the amount of 1.2 mg/cm3 and 5 mg/cm3, respectively.In order to obtain fragments of peptidoglycans of cell walls of probiotic bacteria as potential bioligands for complex formation, their enzymatic hydrolysis with pancreatin has been performed. It has been established that the highest content of biologically active muropeptides is 5.1 mg/cm3 and it is accumulated during hydrolysis of the substrate for 180 minutes, the ratio of enzyme: substrate 1: 100 and 5.1 mg/cm3.By methods of nephelometry and spectrophotometry, it has been established that the obtained mixed ligand systems are effective chelating agents and, depending on the composition, bind calcium in amounts of 9, 14 and 16 mg/cm3. Identification of the pH stability of the complex has been shown that in the range of pH values 4–7, the chelate system is stable, at pH 2 only 10% of the complex is stored, at pH 9 60% is preserved. By method of differential scanning calorimetry the thermostability of the complex has been investigated. It has been established that the complex is stable in the temperature range of 20–122°С, and therefore can be used in the composition of health foods, the technology of which involves high-temperature processing.
The food industry is a strategic industry that works quite steadily even during periods of economic crises, providing food security to any state, and is a source of raw material for other industries with a high potential for development, for example, for the production of cosmetics. The modern cosmetics market is represented by various cosmetic products, often expensive, but not always made from natural ingredients. Therefore, the search for the newest ingredients for the production of natural cosmetics on the basis of domestic raw materials is an urgent task of the present. Ingredients from milk serum can be used for the production of natural cosmetics that in large quantities is obtained in milk processing enterprises and often remains unprocessed. Whey protein concentrations can be a source of short-chain peptides and free amino acids for the production of various cosmetic products. The process of fermentolysis of serum proteins in nanofiltration concentrate KSB-65 with the content of dry matter of 20% using neutral peptidase C from the domestic producer at a temperature of 40 ºС with the duration of the process varying from 1 to 5 hours, the content of peptidase – from 0,5 to 2,0 U/g. It is established that the optimal parameters of the fermentolysis of serum proteins in KSB-65 are as follows: temperature 40 º C, neutral peptidase C content – 0.78 U/g, duration of fermentolysis – 3.17 hours. With optimal parameters of the fermentolysis process, the hydrolyzate of the nanofiltration concentrate KSB-65 contains the maximum amount of short chain peptides (57.03 mg/cm3) and a high concentration of free amino acids (54.66 μg/cm3). Recommendations for the further use of serum protein hydrolyzate obtained using the recommended optimal parameters of the enzyme production process from the nanofiltration concentrate KSB-65, in the manufacture of cosmetic products, including with anti-age effect, and hydrolyzates of proteins enriched with probiotic cultures of lactam bifidobacteria or their lysates.
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