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Nucleic Acids Symposium Series 2006 50(1):253-254; doi:10.1093/nass/nrl126
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© 2006 Oxford University Press

Improvement of binding activity of xylan-binding domain by amino acid substitution

Tomoko Sakata, Jun Takakura, Hiroyuki Miyakubo, Yuko Osada, Rieko Wada, Hidenori Takahashi, Rie Yatsunami, Toshiaki Fukui and Satoshi Nakamura

Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan

Xylanase J (XynJ) of alkaliphilic Bacillus sp. strain 41M-1 is a multi-domain enzyme and consists of a glycoside hydrolase (GH) family 11 catalytic domain and an additional xylan-binding domain (XBD) belonging to carbohydrate-binding module (CBM) family 36. Random mutations were introduced into the XBD gene and the repertoire was cloned for display on the surface of filamentous phage. The mutant XBD with amino acid substitution T316I (Thr317 was replaced by Ile) showed higher xylan-binding activity compared to the wild-type XBD. Furthermore, hydrolyzing activity of XynJ toward insoluble xylan was also improved by introducing the mutation T316I.


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