Abstract
The physico-chemical properties of oat proteins (globulins) were determined and an analysis was done whether products of in silico proteolysis contain mono- and multi-functional peptides with various biological activity. The MW(s), calculated by the ProtParam program, for precursors of 12S and 11S globulins and proteins without signal peptides were in the range of 50.78–61.86 kDa. The pH at which the solubility of the proteins under analysis was the lowest ranged from 7.29 to 9.44. A simulation of proteolysis with three enzymes (pepsin, trypsin, and chymotrypsin A) in the optimum conditions of the enzyme action can produce 6–8 bi-functional, 5–10 mono-functional biopeptides from oat globulins (12S, 11S globulins), and one tri-functional biopeptide (VY). The mono-functional biopeptides exhibited the activity of DPPIV inhibitors or ACE inhibitors, and the multi-functional biopeptides can exhibit the activity of inhibitors of both enzymes (DPPIV and ACE). Sensory peptides accounted for 43% of all the released mono- and multi-functional biopeptides.
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