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Controlled enzymatic hydrolysis of glycinin: susceptibility of acidic and basic subunits to proteolytic enzymes.

Govindaraju, K. and Srinivas, H. (2007) Controlled enzymatic hydrolysis of glycinin: susceptibility of acidic and basic subunits to proteolytic enzymes. LWT - Food Science and Technology, 40 (6). pp. 1056-1065.

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Abstract

Glycinin, the major storage protein of soyabeans was enzymatically modified using papain, alcalase and fungal protease. The degree of hydrolysis (DH) was monitored by using trinitrobenzene sulfonic acid reaction with liberated alpha-amino groups. The DH could be varied by varying the ratio of enzyme to substrate, time and temperature of hydrolysis. The measured Km and Vmax values of glycinin with different proteases suggested that the susceptibility for hydrolytic cleavage of glycinin followed the order fungal protease > alcalase > papain. Electrophoretic analysis of cleaved glycinin suggested that acidic subunits of glycinin were cleaved preferentially over basic subunits. The measured Km and Vmax with acidic and basic subunits with fungal protease correlated with cleavage susceptibility. The functional properties of glycinin could be tailored by controlling the DH and using appropriate protease. Modified glycinin had better functional characteristics compared to glycinin. All rights reserved, Elsevier.

Item Type: Article
Uncontrolled Keywords: FUNCTIONAL-PROPERTIES; PROTEINASES-; SOY-PROTEINS; SOYBEANS-; TEMPERATURE-; GLYCININ-; HYDROLYSIS-; MODIFICATION-; TEMP.-
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 27 Jun 2011 07:02
Last Modified: 09 Apr 2018 11:10
URI: http://ir.cftri.com/id/eprint/8068

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