Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85.

Applied and Environmental Microbiology
S R MalburgC W Forsberg

Abstract

The celF gene from the predominant cellulolytic ruminal bacterium Fibrobacter succinogenes encodes a 118.3-kDa cellulose-binding endoglucanase, endoglucanase F (EGF). This enzyme possesses an N-terminal cellulose-binding domain and a C-terminal catalytic domain. The purified catalytic domain displayed an activity profile typical of an endoglucanase, with high catalytic activity on carboxymethyl cellulose and barley beta-glucan. Immunoblotting of EGF and the formerly characterized endoglucanase 2 (EG2) from F. succinogenes with antibodies prepared against each of the enzymes demonstrated that EGF and EG2 contain cross-reactive epitopes. This data in conjunction with evidence that the proteins are the same size, share a 19-residue internal amino acid sequence, possess similar catalytic properties, and both bind to cellulose allows the conclusion that celF codes for EG2.

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Citations

Jan 29, 2000·FEMS Microbiology Letters·S Subramaniyan, P Prema
Jul 31, 2007·Applied and Environmental Microbiology·Meng QiCecil W Forsberg
Jan 29, 2000·FEMS Microbiology Letters·M Mitsumori, H Minato
Jan 20, 2009·Applied and Environmental Microbiology·Atsushi ToyodaHajime Minato
Jun 22, 2001·Journal of Dairy Science·J MironM Morrison
Apr 2, 2008·Annals of the New York Academy of Sciences·David B Wilson
May 26, 2017·Scientific Reports·Chia-Wei WuSteven D Brown
Nov 26, 2003·FEMS Microbiology Reviews·Denis O KrauseChristopher S McSweeney
Feb 3, 1998·Trends in Microbiology·H J Flint

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