Catalytic Properties of the Cellulose-binding Endoglucanase F from Fibrobacter Succinogenes S85

Overview

Journal Appl Environ Microbiol

Specialties Environmental Health
Microbiology

Date 1997 Jun 1

PMID 9172367

Citations 15

Authors

S R Malburg

L M Malburg Jr

T Liu

A H Iyo

C W Forsberg

Affiliations

Soon will be listed here.

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.

Citing Articles

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