Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.
Abstract
Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ion-exchange chromatography, size-exclusion chromatography, and reverse-phase high-performance liquid chromatography. The amino acid sequence of this peptide was identified as Ile-Ala-Pro, and the ACE inhibitory activity (IC50 value) was 2.7...
Paper Details
Title
Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.
Published Date
Oct 1, 2003
Journal
Volume
47
Issue
5
Pages
354 - 358
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