Literature DB >> 14609094

Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.

Hirofumi Motoi1, Toshiaki Kodama.   

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 microM. The hypotensive activity of Ile-Ala-Pro on spontaneously hypertensive rats was investigated. This peptide inhibited the hypertensive activity of angiotensin I with intravenous injection, and decreased the blood pressure significantly with intraperitoneal administration.

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Year:  2003        PMID： 14609094     DOI： 10.1002/food.200390081

Source DB:  PubMed          Journal:  Nahrung        ISSN： 0027-769X


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