Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins
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- 作者：Tidarat Toopchama ; Jurriaan J. Mesb ; Harry J. Wichersb ; Sittiruk Roytrakulc ; Jirawat Yongsawatdigula ; jirawat@sut.ac.th" class="auth_mail" title="E-mail the corresponding author
- 关键词：Muscle proteins ; Protein hydrolysates ; ACE inhibitory activity ; Caco-2 permeability ; Tilapia
- 刊名：Food Chemistry
- 出版年：2017
- 出版时间：1 April 2017
- 年：2017
- 卷：220
- 期：Complete
- 页码：190-197
- 全文大小：790 K
文摘
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The highest ACE inhibition was found in the hydrolysates of tilapia mince.
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In vitro gastrointestinal digestion reduced ACE inhibitory activity of the hydrolysate.
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In vitro digestion enhanced the permeability of the peptides across Caco-2 cells.
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The novel transported peptide with the highest ACE inhibition was identified to be MCS.