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Published on: October 16, 2017
A novel catalysis by porcine pepsin in debranching guar galactomannan
Mysore S Shobha1, Lalitha R Gowda2, Rudrapatam N Tharanathan1
1Department of Biochemistry and Nutrition, Central Food Technological Research Institute, Council of Scientific and Industrial Research, Mysore 570 020, India.
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 thereby showing its non-specific catalysis towards glycosidic substrates.
Results And Conclusions:
Use of non-specific inhibitors, chemical modification agents and peptide mapping of native and GG--bound pepsin upon proteolytic digestion with Staphylococcus aureus V8 protease revealed the involvement of Asp(138) residue in the catalysis, which was confirmed by computational modelling studies.
General Significance:
Here we show a novel mode of catalysis (other than proteolysis) by porcine pepsin with a different active site residue.
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