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Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase

Paper ID Volume ID Publish Year Pages File Format Full-Text
36702 45142 2005 6 PDF Available
Title
Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
Abstract

Soybean proteins, β-conglycinin and glycinin were hydrolysed by an acid proteinase from Monascus purpureus. The degree of hydrolysis and inhibitory activities of angiotensin I-converting enzyme (ACE) increased with increasing proteolysis time. After 10 h of incubation, the IC50 values of the β-conglycinin and glycinin hydrolysates were determined as 0.126 mg/ml and 0.148 mg/ml, respectively. Four ACE inhibitory peptides were isolated from the soybean protein hydrolysates and identified by protein sequencer. ACE inhibitory peptides isolated from the β-conglycinin hydrolysate were identified as LAIPVNKP (IC50 = 70 μM) and LPHF (670 μM), and those from the glycinin hydrolysate as SPYP (850 μM) and WL (65 μM). The inhibitory activity of SPYP markedly increased after successive digestion by pepsin, chymotrypsin and trypsin in vitro.

Keywords
Angiotensin I-converting enzyme inhibitor; Acid proteinase; Soybean protein hydrolysate; Monascus Purpureus; Tofuyo
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Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 40, Issue 6, May 2005, Pages 2191–2196
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us