Phage display of xylan-binding module of xylanase J from alkaliphilic Bacillus sp. strain 41M-1

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 wer...

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Bibliographic Details
Published inNucleic acids symposium series (1979) no. 44; p. 165
Main Authors Miyakubo, H, Sugio, A, Kubo, T, Nakai, R, Wakabayashi, K, Nakamura, S
Format Journal Article
LanguageEnglish
Published England 2000
Subjects
Bacillus - enzymology
Bacillus - genetics
Catalytic Domain - genetics
Endo-1,4-beta Xylanases
Kinetics
Mutagenesis
Peptide Library
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Xylans - metabolism
Xylosidases - chemistry
Xylosidases - genetics
Xylosidases - metabolism
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Summary: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.
ISSN:0261-3166