嗜碱芽孢杆菌属菌株41M-1木聚糖酶J的木聚糖结合模块的噬菌体展示

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

作者信息

Miyakubo H, Sugio A, Kubo T, Nakai R, Wakabayashi K, Nakamura S

机构信息

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

出版信息

Nucleic Acids Symp Ser. 2000(44):165-6. doi: 10.1093/nass/44.1.165.

DOI:10.1093/nass/44.1.165

PMID:12903320

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.

摘要

来自嗜碱芽孢杆菌属菌株41M-1的木聚糖酶J具有11/G家族催化结构域和一个木聚糖结合模块（XBM）。木聚糖酶J的XBM展示在丝状噬菌体表面。在噬菌体表面表达的XBM保留了与木聚糖的结合活性。通过易错PCR在XBM基因中引入随机突变，并将文库克隆以展示在噬菌体上。对木聚糖结合活性缺陷型突变体的序列分析表明，XBM的苯丙氨酸284和色氨酸317有助于木聚糖结合活性。