Open AccessThe multidomain xylanase Xyn10B as a cellulose‐binding protein in Clostridium stercorarium
Author(s) -
Ali Mursheda K,
Kimura Tetsuya,
Sakka Kazuo,
Ohmiya Kunio
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10622.x
Subject(s) - guanidine , carbohydrate binding module , chemistry , cellulose , xylanase , biochemistry , s layer , hydrochloride , ammonium sulfate precipitation , cellobiose , carboxymethyl cellulose , cellulase , size exclusion chromatography , organic chemistry , enzyme , sodium , gene
The cells of Clostridium stercorarium F‐9 grown on cellobiose bound to insoluble cellulose allomorphs such as phosphoric acid‐swollen cellulose (ASC). Treatment of the cells with 3 M guanidine hydrochloride extracted surface‐layer proteins from the cells and abolished the affinity of the cells for ASC. SDS‐polyacrylamide gel electrophoresis, zymogram, and immunological analyses indicated that one of the major surface layer proteins was Xyn10B, which is a modular xylanase comprising two family 22 carbohydrate‐binding modules (CBMs), a family 10 catalytic domain of glycosyl hydrolases, a family 9 CBM, and two S‐layer homologous (SLH) domains. The C. stercorarium F‐9 cells treated with guanidine hydrochloride coprecipitated with ASC upon the addition of a derivative of Xyn10B containing both a CBM and SLH domain in addition to a catalytic domain, but not a derivative without Xyn10B‐SLH domains, suggesting that Xyn10B functioned as a cellulose‐binding protein in C. stercorarium F‐9.