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Angiotensin I-converting enzyme inhibitory peptides in red-mold rice made by Monascus purpureus

Paper ID Volume ID Publish Year Pages File Format Full-Text
35066 45071 2009 5 PDF Available
Title
Angiotensin I-converting enzyme inhibitory peptides in red-mold rice made by Monascus purpureus
Abstract

The ACE inhibitory activity in red-mold rice extracts, prepared from 24 strains of the genus Monascus, was measured. The most effective strain for ACE inhibition was Monascus purpureus IFO 4489 (IC50 = 0.71 mg/ml). Although the antihypertensive substance γ-amino butyric acid was detected in the red-mold rice (85.2 mg/kg), it did not contribute to ACE inhibition. Four ACE inhibitory peptides were isolated from the extract and identified as Ile-Tyr (IC50 = 4.0 μM), Val-Val-Tyr (22.0 μM), Val-Phe (49.7 μM) and Val-Trp (3.1 μM) by protein sequencing. The ACE inhibitory activity of these peptides was almost completely preserved after successive in vitro digestion by pepsin, chymotrypsin and trypsin. These results suggest that red-mold rice made by M. purpureus could be useful in alleviating hypertension.

Keywords
Red-mold rice; Monascus purpureus; Angiotensin I-converting enzyme inhibitor; Hypertension; Bioactive peptide; Tofuyo
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 10, October 2009, Pages 1139–1143
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