Affiliation
a Kemerovo State University
Copyright ©Milentyeva et al. This is an open access article distributed under the terms of the Creative Commons Attribution 4.0. (
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Abstract
Results of biotechnological research on controlled hydrolysis of casein and production of peptide complexes are summarized in the present article. Selection of processing parameters and optimization of the conditions of enzymatic hydrolysis of milk proteins allowed for the development of a resource-efficient technology for the production of peptide complexes. Enzymatic hydrolysis of peptide bonds R1-CONH-R2 + H2O - R1COOH + NH2R2 was considered using the example of casein and a range of proteolytic enzymes (trypsin and chymotrypsin) belonging to the hydrolase class. Enzyme solution (0.1% m/v) was added to each protein solution so that the final enzyme-substrate ratio was 1:25, 1:50, or 1:100. The enzyme-substrate ratio of 1:50 was shown to be optimal, and the re-commended temperature and pH values were 50±1°С and 7.50±0.01, respectively. The degree of hydrolysis is one of the parameters characterizing the overall changes in the amino acid composition of proteins. Therefore, a time period of 12.00±0.05 h was chosen as the optimal duration of the hydrolysis process. Further research was focused on the analysis of peptide profiles using MALDI-TOF MS based on identification of peptide sequences. The studies have shown that casein hydrolysates are rich in biologically active peptide complexes. The detection of such complexes in hydrolysates of casein was the main result of the study. For example, the peptide β-casokinin (amino acid sequence Ala-Val-Pro-Tyr-Pro-Gln-Arg) is an inhibitor of angiotensin-converting enzyme.
Keywords
casein,
enzyme preparations,
peptides,
prevention,
hypertensive disease,
chronic cardiac insufficiency
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