Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1190800 | Food Chemistry | 2007 | 6 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Vasudeva Kamath, Sajeeda Niketh, Arun Chandrashekar, P.S. Rajini,