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A novel catalysis by porcine pepsin in debranching guargalactomannan.

Shobha, M. S. and Gowda, L. R. and Tharanathan, R. N. (2014) A novel catalysis by porcine pepsin in debranching guargalactomannan. Carbohydrate Polymers, 102. pp. 615-621.

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Abstract

Background: Pepsin (porcine stomach mucosa, E.C. 3.4.23.1), an acid protease catalyzes the hydrolysis(debranching) of guar galactomannan (GG), a co-polymer of mannose and galactose residues therebyshowing its non-specific catalysis towards glycosidic substrates.Results and conclusions: Use of non-specific inhibitors, chemical modification agents and peptide mappingof native and GG – bound pepsin upon proteolytic digestion with Staphylococcus aureus V8 proteaserevealed the involvement of Asp138residue in the catalysis, which was confirmed by computationalmodelling studies.General significance: Here we show a novel mode of catalysis (other than proteolysis) by porcine pepsinwith a different active site residue.

Item Type: Article
Uncontrolled Keywords: Porcine pepsin Guar galactomannan Non-specificity Peptide mapping Active site Docking
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
Divisions: Dept. of Biochemistry
Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 23 Jan 2014 07:27
Last Modified: 23 Jan 2014 07:27
URI: http://ir.cftri.com/id/eprint/11328

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