PMID: 11325557Apr 28, 2001Paper

The multidomain xylanase Xyn10B as a cellulose-binding protein in Clostridium stercorarium

FEMS Microbiology Letters
M K AliK Ohmiya

Abstract

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.

References

Jan 1, 1995·Advances in Microbial Physiology·P TommeN R Gilkes
Jun 5, 1999·Extremophiles : Life Under Extreme Conditions·D D MorrisP L Bergquist
Sep 3, 1999·Applied and Environmental Microbiology·A E CazemierH J Op den Camp
Mar 29, 2001·Bioscience, Biotechnology, and Biochemistry·M K AliK Ohmiya

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Citations

Oct 29, 2003·The Journal of General and Applied Microbiology·Atsushi ToyodaHajime Minato
Jul 25, 2006·Bioscience, Biotechnology, and Biochemistry·Guangshan ZhaoKazuo Sakka
Nov 25, 2005·Bioscience, Biotechnology, and Biochemistry· Si Si HlaKazuo Sakka
Dec 18, 2007·Journal of Bacteriology·Wolfgang LieblMichael Valdez
Jul 26, 2005·Applied Microbiology and Biotechnology·Guangshan ZhaoKazuo Sakka

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