Keywords

Peptides, Angiotensin-Converting Enzyme (Ace), Spirulina, Selenium

Abstract

Total protein (SeSP-TP) was extracted from Selenium-rich Spirulina (SeSP), SeSP-TP was hydrolyzed with different proteases to prepare Selenium-rich Spirulina polypeptides (SeSP-Ps), and the effect of SeSP-Ps on angiotensin-converting enzyme (ACE) was determined in vitro. ) inhibitory effect. The results show that the degree of hydrolysis of SeSP-TP by five common proteases is significantly different under optimal conditions, among which the degree of enzymatic hydrolysis is the highest when pepsin-trypsin-chymotrypsin is used in combination; although SeSP-Ps prepared by hydrolysis by different proteases All have strong inhibitory effects on ACE, but there are obvious differences in the 50% inhibitory concentration (IC50) of SeSP-Ps hydrolyzed by different enzymes on ACE. Among them, SeSP-Ps prepared by combined enzymatic hydrolysis of pepsin-trypsin-chymotrypsin Ps has the lowest IC50 value for ACE, which is 74.6 ¦Ìg/mL. The results suggest that the peptides produced by SeSP through gastrointestinal protease digestion in vivo have strong inhibitory activity against ACE, and the inhibitory effect of SeSP-Ps on ACE shows a significant dose-effect dependence.

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Original research done by Ling Qinjie, Zhang Yibo, Zou Ying, Gao Dongfang, Huang Zhi

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