Article ID Journal Published Year Pages File Type
1190800 Food Chemistry 2007 6 Pages PDF
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
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