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A Calcium-Dependent Xylan-Binding Domain of Alkaline Xylanase from AlkaliphilicBacillussp. Strain 41M-1
Author(s) -
Risa Yazawa,
Jun Takakura,
Tomoko Sakata,
Ihsanawati Ihsanawati,
Rie Yatsunami,
Toshiaki Fukui,
Takashi Kumasaka,
Nobuo Tanaka,
Satoshi Nakamura
Publication year - 2011
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.100730
Subject(s) - xylan , xylanase , strain (injury) , chemistry , carbohydrate binding module , biochemistry , microbiology and biotechnology , food science , enzyme , biology , glycoside hydrolase , anatomy
Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca(2+)-dependent xylan-binding, and that Asp313 and Asp318 were especially important.

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