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

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

Bioscience Biotechnology and Biochemistry · 2009 · 43 citations · 8 references

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Abstract

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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