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Study Of Angiotensin Ⅰ Converting Enzyme Inhibitory Peptides From Enzymic Hydrolysates Of Acaudina Molpadioidea Collagen

Posted on:2007-12-02Degree:MasterType:Thesis
Country:ChinaCandidate:Y H ZhaoFull Text:PDF
GTID:2121360185990576Subject:Aquatic Products Processing and Storage Engineering
Abstract/Summary:PDF Full Text Request
Extraction of collagen from Acaudina Molpadioidea body wall, enzymic hydrolysis conditions of collagen, purification and partial characterization of angiotensinⅠconverting enzyme(ACE) inhibitory peptides from enzymic hydrolysates were studied in this paper.Extraction yield of collagen with acid, enzyme, hot water was 4.72%,29.30% and 53.50%, respectively. The results showed that extraction with hot water was superior to other methods. Therefore extraction of collagen from Acaudina Molpadioidea with hot water method was used in this study.The crude ACE was successfully extracted from hog lung through immersed with Tris-HCl buffer solution and deposited with ammonium sulfate and separated by Sephadex G-200. The specific activity of crude ACE was 63.36u.papain, trypsin, 3942 neutral proteinase, bromelain, collagenase and alcalase were used to hydrolyze Acaudina Molpadioidea collagen, respectively.Based on the IC50 values of six kinds of single enzymic hydrolysates, bromelain, alcalase, and collagenase were selected as compound enzyme. The most optimal enzymic hydrolysis conditions of three kinds of single enzyme were determined by orthogonal test. The results showed as follows: 45℃, pH4.5, substrate concentration 1.0%, enzyme dosage 2000U/g, time 4h for bromelain; 55℃, pH 7.4, substrate concentration 1.5%, enzyme dosage 2000U/g, time 2h for alcalase; 37℃,pH 7.4, substrate concentration 1.0%, enzyme dosage 1500U/g, time 4h for collagenase, respectively. Collagen were hydrolyzed by serial...
Keywords/Search Tags:Acaudina Molpadioidea, collagen, ACE inhibitory peptides, compound enzymic hydrolysis, isolation and purification
PDF Full Text Request
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