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

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

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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.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Ltd.
Uncontrolled Keywords:	Sorghum flour; Angiotensin converting enzyme; Kafirin; Chymotryptic hydrolysate; IC50; Lineweaver–Burk plots
Subjects:	600 Technology > 08 Food technology > 21 Cereals
Divisions:	Food Protectants and Infestation Control
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	07 Apr 2007
Last Modified:	28 Dec 2011 09:27
URI:	http://ir.cftri.res.in/id/eprint/542

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