Improvement of Alkaliphily of Bacillus Alkaline Xylanase by Introducing Amino Acid Substitutions Both on Catalytic Cleft and Protein Surface

Hirohito UMEMOTO; IHSANAWATI; Mayuko INAMI; Rie YATSUNAMI; Toshiaki FUKUI; Takashi KUMASAKA; Nobuo TANAKA; Satoshi NAKAMURA

doi:10.1271/bbb.80869

This article has now been updated. Please use the final version.

Improvement of Alkaliphily of Bacillus Alkaline Xylanase by Introducing Amino Acid Substitutions Both on Catalytic Cleft and Protein Surface

Hirohito UMEMOTO, IHSANAWATI, Mayuko INAMI, Rie YATSUNAMI, Toshiaki FUKUI, Takashi KUMASAKA, Nobuo TANAKA, Satoshi NAKAMURA

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Keywords: xylanase, alkaliphily, glycoside hydrolase (GH) family 11, Bacillus sp.

JOURNAL FREE ACCESS Advance online publication

Article ID: 80869

DOI https://doi.org/10.1271/bbb.80869

The final version of this article is now available: Vol. 73 (2009) , No. 4 p.965

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Abstract

Xylanase J (XynJ) from alkalipilic 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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