ISOLATION FROM ALPHA-ZEIN OF THERMOLYSIN PEPTIDES WITH ANGIOTENSIN I-CONVERTING ENZYME-INHIBITORY ACTIVITY

Authors
YANO S SUZUKI K FUNATSU G
Citation
S. Yano et al., ISOLATION FROM ALPHA-ZEIN OF THERMOLYSIN PEPTIDES WITH ANGIOTENSIN I-CONVERTING ENZYME-INHIBITORY ACTIVITY, Bioscience, biotechnology, and biochemistry, 60(4), 1996, pp. 661-663
Citations number
6
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
60
Issue
4
Year of publication
1996
Pages
661 - 663
Database
ISI
SICI code
0916-8451(1996)60:4<661:IFAOTP>2.0.ZU;2-V
Abstract
Urea-denatured alpha-zein was almost completely hydrolyzed into small peptides by digestion with 1/100 (w/w) of thermolysin at 37 degrees C for 3 h. The angiotensin I-converting enzyme (ACE) inhibitory activity (IC50) of the thermolysin digest of total alpha-zein was 24.5 mu g/ml , and most of the peptide fractions from Z19 alpha-zein and total alph a-zein separated by reverse-phase HPLC had more or less ACE inhibitory activity. From these fractions, thirty-six peptides, including 5 dipe ptides, 14 tripeptides, 9 tetrapeptides, 5 pentapeptides, acid 3 hexap eptides, were purified and their amino acid sequences were determined.