Abstract
In this study, two novel mixed ACE-inhibiting peptides, namely Se-TAPep 1 and TAPep 1, were prepared and purified from selenium-enriched and common alkali-soluble proteins using a series of process, and then its physicochemical properties and oligopeptide sequence were analyzed. The results showed that Se-TAPep 1 and TAPep 1 could be successfully separated, but their ACE inhibitory activities were different (IC50 values were 13.39 mg/mL and 23.56 mg/mL, respectively), this may be related to the difference in selenium content. Further analysis of physicochemical properties showed that the protein or peptide fractions contained their characteristic absorption peaks and contained aromatic amino acids, while the apparent morphology was different, the presence of selenium could change the apparent morphology of protein or polypeptide fractions, arranging of selenium-enriched fractions more irregular. The amino acid composition analysis showed that the Pro content of the selenium-enriched fractions was higher than that of the ordinary component, whereas the oligopeptide sequence analysis showed that both LQPSLGFP derived from Se-TAPep 1 and AETGEIKGHY derived from TAPep 1 contained some characteristics of highly active ACE-inhibiting peptides, but the characteristics of LQPSLGFP were more conspicuous, which may be related to its molecular weight and source of mixed peptides. These findings indicated that the selenium-enriched tea mixed peptides had better potential uses than ordinary tea mixed peptides in the preparation of functional food.
Published Version
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