title: Preparation of ACE inhibitory peptides from Mytilus coruscus hydrolysate using uniform design.
abstract: The angiotensin-I-converting enzyme (ACE) inhibitory peptides from mussel, Mytilus coruscus, were investigated and the variable factors, protease concentration, hydrolysis time, pH, and temperature, were optimized using Uniform Design, a new statistical experimental method. The results proved that the hydrolysate of alkali proteases had high ACE-inhibitory activity, especially the alkali protease E1. Optimization by Uniform Design showed that the best hydrolysis conditions for preparation of ACE-inhibitory peptides from Mytilus coruscus were protease concentration of 36.0 U/mL, hydrolysis time of 2.7 hours, pH 8.2, and Temperature at 59.5°C, respectively. The verification experiments under optimum conditions showed that the ACE-inhibitory activity (91.3%) were agreed closely with the predicted activity of 90.7%. The amino acid composition analysis of Mytilus coruscus ACE-inhibitory peptides proved that it had high percent of lysine, leucine, glycine, aspartic acid, and glutamic acid.
authors.affiliation: Second Institute of Oceanography, SOA, Hangzhou 310012, China. superwujc@yahoo.com.cn
authors.forename: Jin-Chao
authors.initials: JC
authors.lastname: Wu
authors.forename: Jie
authors.initials: J
authors.lastname: Cheng
authors.forename: Xiao-lai
authors.initials: XL
authors.lastname: Shi
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D000818:Animals; D006801:Humans; D006868:Hydrolysis; D049878:Mytilus / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry* / Q000302:isolation & purification*; D010447:Peptide Hydrolases / Q000737:chemistry; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; D010447:Peptide Hydrolases; C488034:ACE protein, human; D007703:Peptidyl-Dipeptidase A