Characterization of Nocardiopsis -1,3-glucanase with additional carbohydrate-binding domains | Zendy

Nobuo Koizumi | Zendy; Yuya Isoda | Zendy; K Maeda | Zendy; Shinji Masuda | Zendy; G. Fibriansah | Zendy; Takashi Kumasaka | Zendy; Rie Yatsunami | Zendy; Toshiaki Fukui | Zendy; Sho Nakamura | Zendy

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Characterization of Nocardiopsis -1,3-glucanase with additional carbohydrate-binding domains

Author(s) -

Nobuo Koizumi,

Yuya Isoda,

K Maeda,

Shinji Masuda,

G. Fibriansah,

Takashi Kumasaka,

Rie Yatsunami,

Toshiaki Fukui,

Sho Nakamura

Publication year - 2007

Publication title -

nucleic acids symposium series

Language(s) - English

Resource type - Journals

eISSN - 1746-8272

pISSN - 0261-3166

DOI - 10.1093/nass/nrm230

Subject(s) - glucanase , bacillus circulans , carbohydrate binding module , chitinase , biochemistry , enzyme , binding domain , chemistry , biology , microbiology and biotechnology , binding site , glycoside hydrolase

beta-1,3-Glucanase F (BglF) from alkaliphilic Nocardiopsis sp. F96 is a single domain enzyme composed of only a catalytic domain. Chimeric BglFs with some carbohydrate-binding domains were constructed and characterized. By connecting the C-terminal additional domain of beta-1,3-glucanase H from Bacillus circulans IAM1165 and the chitin-binding domain of chitinase J from alkaliphilic Bacillus sp. J813, binding ability and hydrolyzing activity toward insoluble beta-1,3-glucans were both improved.

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