BIOLOGICALLY ACTIVE PEPTIDES AND FUNCTIONAL AND TECHNOLOGICAL PROPERTIES OF RAPESEED PROTEIN HYDROLYSATES

Biologically active peptides with a given activity can be obtained by directed enzymatic hydrolysis of proteins. There is a large amount of information in scientific literature on the production of biologically active peptides from animal raw materials, while plant sources are almost not considered. Among oilseeds and legumes, rapeseed has one of the greatest potentials in protein production, which amounts to about 13.8 million tons per year, as well as in the production of biologically active peptides based on it. The aim of the work was to study the patterns of hydrolysis of rapeseed protein isolate under the action of commercial enzyme preparations (AF) proteases to form peptides with predicted biological activity. It was shown that, in comparison with the rapeseed protein isolate, the FCS was most significantly increased in samples of hydrolysates with a protein hydrolysis rate of 10% obtained using Alcalase 2.4 L FG, SQzyme PS and Sunson neutral. The increase in moisture-binding capacity averaged 14%, fat-binding capacity 89%, fat-emulsifying properties 7%, and emulsion resistance 8%. The foaming capacity increased by an average of 47%, while the foam resistance decreased by 25%. By the LC-MS/MS method, 6667 peptides were determined in hydrolysates obtained using Alcalase 2.4 L FG, of which 4 were major, 7678 peptides in a sample of hydrolysate obtained using SQzyme PS, among which 3 were major, and 9034 peptides in a sample with Sunson neutral for which 6 major peptides were selected. Using bioinformatic database tools, 13 ACE inhibitor peptides with antitumor and hypoglycemic activities, 11 peptides with potential antioxidant and antihypertensive activities, 2 peptides with antithrombotic properties, and 5 alpha-glucosidase inhibitors were identified among the major peptides. No potentially allergenic peptides were found. For the gilrolysates obtained using the drug "Alcalase 2.4 L FG", 2 potential bitter peptides out of 4 were identified, using the drug "SQzyme PS", 3 of the 3 peptides were identified as bitter, using the drug "Sunson neutral", 4 bitter peptides out of 6 were predicted. The selected peptides can then be obtained synthetically and examined for targeted biological activity during empirical studies. The synthesis of individual peptides eliminates impurities and variability in terms of the qualitative composition of peptides in hydrolysates, as well as ensures their purity and stability of the target biological activity.