Abstract
Xylanase J from alkaliphilic Bacillus sp. strain 41M-1 has a family 11/G catalytic domain and a xylan-binding module (XBM). The XBM of xylanase J was displayed on the surface of filamentous bacteriophage. The XBM expressed on the phage surface retained binding activity to xylan. Random mutations were introduced in the XBM gene by error-prone PCR, and the repertoire was cloned for display on phage. Sequence analysis of the xylan-binding activity-deficient mutants revealed that Phe 284 and Trp317 of the XBM would contribute to the xylan-binding activity.
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