Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ
✍ Scribed by Toshiro Matsui; Chun-Hui Li; Yutaka Osajima
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 124 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1075-2617
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✦ Synopsis
Reported is the preparation of wheat germ (WG) hydrolyzate with potent angiotensin I-converting enzyme (ACE) inhibitory activity, and the characterization of peptides responsible for ACE inhibition. Successful hydrolyzate with the most potent ACE inhibitory activity was obtained by 0.5 wt.% -8 h Bacillus licheniformis alkaline protease hydrolysis after 3.0 wt.% -3 h h-amylase treatment of defatted WG (IC 50 ; 0.37 mg protein ml -1 ). The activity of WG hydrolyzate was markedly increased by ODS and subsequent AG50W purifications (IC 50 ; 0.018 mg protein ml -1 ). As a result of isolations by high performance liquid chromatographies, 16 peptides with the IC 50 value of less than 20 mM, composed of 2 -7 amino acid residues were identified from the WG hydrolyzate. Judging from the high content (260 mg in 100 g of AG50W fraction) and powerful ACE inhibitory activity (IC 50 ; 0.48 mM), Ile-Val-Tyr was identified as a main contributor to the ACE inhibition of the hydrolyzate.