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 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.
Miyakubo
H
H
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Sugio
A
A
Kubo
T
T
Nakai
R
R
Wakabayashi
K
K
Nakamura
S
S
D001407:Bacillus / Q000201:enzymology* / Q000235:genetics*; D020134:Catalytic Domain / Q000235:genetics; D043364:Endo-1,4-beta Xylanases; D007700:Kinetics; D016296:Mutagenesis; D019151:Peptide Library; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014990:Xylans / Q000378:metabolism; D014995:Xylosidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D019151:Peptide Library; D011993:Recombinant Fusion Proteins; D014990:Xylans; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases