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Article

Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface.

Bioscience, biotechnology, and biochemistry - 23 Apr 2009

Umemoto Hirohito, Ihsanawati, Inami Mayuko, Yatsunami Rie, Fukui Toshiaki, Kumasaka Takashi, Tanaka Nobuo, Nakamura Satoshi

Abstract excerpt

Xylanase J (XynJ) from alkaliphilic Bacillus sp. 41M-1 is an alkaline xylanase. The crystal structure has been solved with XynJ. Improvement of the alkaliphily of XynJ was attempted by amino acid substitutions. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shifted the optimum pH of the wild-type enzyme from 8.5 to 9.5.

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19352020
DOI: 10.1271/bbb.80869

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