1. Catalytic properties of the cellulose-binding endoglucanase F from Fibrobacter succinogenes S85.
- Author
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Malburg SR, Malburg LM Jr, Liu T, Iyo AH, and Forsberg CW
- Subjects
- Amino Acid Sequence, Animals, Binding Sites, Cellulase chemistry, Cellulase genetics, Cellulose metabolism, Genes, Bacterial, Gram-Negative Anaerobic Bacteria genetics, Molecular Sequence Data, Molecular Weight, Restriction Mapping, Rumen microbiology, Sequence Homology, Amino Acid, Cellulase metabolism, Gram-Negative Anaerobic Bacteria enzymology
- 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.
- Published
- 1997
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