Structure and Function of a Multidomain Alkaline Xylanase from Alkaliphilic Bacillus Sp. Strain 41M-1 |
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Authors: | Satoshi Nakamura |
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Affiliation: | (1) Department of Bioengineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan |
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Abstract: | Xylanase is an enzyme that catalyzes the hydrolysis of xylan, a -1,4-linked xylose polymer. Alkaliphilic Bacillus sp. strain 41M-1 secretes a xylanase (xylanase J) that has an alkaline pH optimum. Xylanase J is a multidomain enzyme and consists of two functional domains: a family 11/G catalytic domain and a non-catalytic xylan-binding domain. The xylan-binding domain bound to xylan and enhanced catalytic activity of the adjacent catalytic domain. Mutational analyses revealed some amino acid residues that contribute to catalytic activity, alkaliphily and xylan-binding activity of xylanase J. |
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Keywords: | xylanase catalytic domain xylan-binding domain alkaliphilic Bacillus sp. |
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