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Glycine-assisted enhancement of 1,4-β-d-xylan xylanohydrolase activity at alkaline pH with a pH optimum shift

  • Vinod Vathipadiekal , Anamika Verma and Mala Rao
Published/Copyright: January 10, 2007
Biological Chemistry
From the journal Volume 388 Issue 1

Abstract

This is the first report describing the enhancement of xylanase activity by the neutral amino acid glycine. Xylanase activity is increased seven-fold at alkaline pH in the presence of glycine and its pH optimum is shifted from pH 7 to 8 without using any protein engineering techniques. Analysis of the steady-state kinetics revealed that glycine in the reaction mixture increases the Km and kcat values of the enzyme. Chemoaffinity labeling and studies using glycine esters indicate an involvement of the carboxylate ion of glycine in enhancing xylanase catalytic activity. A novel possible mechanism for the glycine-assisted catalytic action of xylanase is proposed.

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Published Online: 2007-01-10
Published in Print: 2007-01-01

©2007 by Walter de Gruyter Berlin New York

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