Effects Of Pretreatment On Collagen Hydrolysis And Release Of Angiotensin-Converting Enzyme Inhibitory Peptides
Keywords
Trypsin, Collagen, Pretreatment, Hydrolysis, Ace Inhibitory Activity
Abstract
Trypsin was used as a tool enzyme to study the effects of short-term heat treatment and ultrahigh pressure treatment on collagen hydrolysis and the release of angiotensin-converting enzyme (ACE)-inhibited peptides. The results show that heat treatment can significantly promote the hydrolysis of collagen by trypsin and the release of ACE inhibitory active peptides. The degree of hydrolysis (DH) of the hydrolyzate in the ultrahigh pressure treatment group is not significantly different from that in the untreated group, and the ACE inhibitory activity is significantly lower. in the no treatment group. Research on the relationship between hydrolyzate DH and ACE inhibitory activity shows that during trypsin hydrolysis of collagen, when the degree of hydrolysis is less than 5%, the ACE inhibition rate shows a significant upward trend with the degree of hydrolysis. When the degree of hydrolysis is greater than 5%, the upward trend is no longer obvious. . Peptide mapping analysis further proved that heat treatment can effectively promote the hydrolysis of collagen, and ultrahigh pressure treatment can change the action site of trypsin. Sequence analysis of the hydrolyzate of the heat treatment group showed that the obtained sequences were all derived from the collagen triple helix region, and most of the sequences had potential ACE inhibitory activity. This shows that short-term heat treatment can effectively destroy the triple helix structure of collagen and promote the release of ACE inhibitory peptides.
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Original research was done by Liu Yi, Zhang Yuhao, Ma Liang
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