Open AccessGene sequence analysis and properties of EGC, a family E (9) endoglucanase from Fibrobacter succinogene s BL2
Author(s) -
Béra Christel,
Broussolle Véronique,
Forano Evelyne,
Gaudet Geneviève
Publication year - 1996
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.1574-6968.1996.tb08028.x
Subject(s) - fibrobacter succinogenes , cellulase , gene , enzyme , peptide sequence , biochemistry , chemistry , amino acid , sequence (biology) , nucleic acid sequence , biology , fermentation , rumen
The endoglucanase gene ( endC ) of Fibrobacter succinogenes BL2 encodes a protein of 620 amino acids (EGC) that shows similarity with family El cellulases, and particularly with EGB from F. succinogenes S85. Alignment of the amino acid sequence of family El cellulases revealed that EGC is composed of a N‐terminal domain and a large catalytic domain of 453 residues containing an extension of 60 residues at its C‐terminal part which is not present in other family El enzymes. EGC shows the same substrate specificity as EGB, and is also inhibited by EDTA. However, its optimal pH (7.0) and temperature (37°C) for activity are different.