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Chymotryptic hydrolysates of a-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity.

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Relation http://ir.cftri.com/542/
http://www.sciencedirect.com/science/journal/03088146
10.1016/j.foodchem.2005.10.004
 
Title Chymotryptic hydrolysates of a-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity.
 
Creator Vasudeva, Kamath
Sajeeda, Niketh
Chandrashekar, A.
Rajini, P. S.
 
Subject 21 Cereals
 
Description Kafirin is the main storage protein (prolamin) in sorghum grains. α-Kafirin, the alcohol soluble fraction, was isolated from sorghum flour. Treatment of α-kafirin with chymotrypsin yielded a hydrolysate which on fractionation, using Sephadex G-25 column, yielded four fractions with significant angiotensin converting enzyme (ACE) inhibitory activity in vitro. The IC50 values of these fractions ranged from 1.3 to 24.3 μg/ml. Two of the fractions were found to be competitively inhibiting the enzyme, while two other fractions were non-competitive inhibitors. These results demonstrate that chymotryptic hydrolysates of sorghum prolamin could serve as a good source of peptides with angiotensin I converting enzyme inhibitory activity.
 
Date 2006
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/542/1/Food_Chemistry_100_%282007%29_306-311.pdf
Vasudeva, Kamath and Sajeeda, Niketh and Chandrashekar, A. and Rajini, P. S. (2006) Chymotryptic hydrolysates of a-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity. Food Chemistry, 100 (1). pp. 306-311. ISSN 0308-8146