Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 52, Issue 4, Pages 771-775Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf0350865
Keywords
angiotensin I-converting enzyme inhibitory peptide; inhibitory profile; kinetics; peptic digestion; porcine skeletal troponin C
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A novel angiotensin I-converting enzyme (ACE) inhibitory peptide (RMLGQTPTK; 9mer) from porcine skeletal troponin C was investigated for its inhibitory profile. This peptide was noncompetitive and as hydrophobic as the known ACE inhibitory peptides. Aminopeptidase M quickly hydrolyzed 9mer, resulting in production of MLGQTPTK and LGQTPTK with inhibitory activities similar to those of 9mer. The main hydrolysis product of 9mer with carboxypeptidase A and B was RMLGQTPT showing very weak activity. Most products derived from 9mer hydrolysis by ACE, aminopeptidase, or carboxypeptidase showed weak but definite ACE inhibitory activities. Thus, 9mer was estimated to be a wholly efficient inhibitor with these fragment peptides.
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