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

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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

著者情報

キーワード: xylanase, alkaliphily, glycoside hydrolase (GH) family 11, Bacillus sp.

ジャーナルフリー早期公開

論文ID: 80869

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

この記事には本公開記事があります。

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

詳細

抄録

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.

責任著者(Corresponding author)

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