Keywords

Soy Protein Isolate, Protease, Angiotensin-Converting Enzyme Activity Inhibition, Ultrafiltration Separation

Abstract

Study the differences in the inhibition of angiotensin-converting enzyme (ace) activity of enzymatic peptides acted on by different proteases, and the relationship between the degree of hydrolysis, molecular weight distribution and ace inhibition rate of enzymatic hydrolysis products. Five proteases, including trypsin, pepsin, neutral protease, papain, and alkaline protease, were used to proteolyze soybean separation, and experiments were conducted on peptide increment, hydrolysis degree, ultrafiltration membrane separation, and comparison of its ace inhibition rate. The results show that alkaline protease has the largest increase in peptides, followed by pepsin, papain and neutral protease, while trypsin has an abnormality; the degree of hydrolysis increases with the time of enzymatic hydrolysis, and the maximum degree of hydrolysis of alkaline protease It can reach 21%, followed by pepsin, papain and neutral protease, with the lowest trypsin being only about 9%; correspondingly, the enzymatic hydrolyzate of alkaline protease has the highest ACE activity inhibition rate (44.9%). Pepsin followed (43.5%). Components with a molecular weight range below 1000da have the highest inhibitory effect on ace. The composition of small molecule peptides obtained by alkaline protease is 71.25%, and that of pepsin is 69.35%, but their corresponding ace inhibition rates are 64.57% and 78.49%. The ace inhibition rates of small molecule peptides obtained by neutral protease, papain and trypsin were 45.7%, 47.3% and 29.6% respectively. Pepsin has the best effect in preparing antihypertensive peptides, followed by alkaline protease, papain, neutral protease and trypsin.

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Original research done by Fan Yuanjing, Ji Yingying, Zhang Yan

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