Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
19302 | Food and Bioproducts Processing | 2006 | 4 Pages |
Abstract
Kinetics of fragmentation of angiotensin-I converting enzyme inhibitory peptides obtained by digestion in gastric juice were studied under intestinal digestion conditions and their inhibitory activities were determined. A fragment IKYGD produced by digestion, as well as IKWGD synthesized, showed similar inhibitory activity to the original peptides. These peptides somehow were resistant to tryptic and/or chymotryptic digestion, and IK + aromatic amino acid might be important functional parts in some kinds of ACE inhibitory peptides.
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