Open AccessIdentification of the cellulose‐binding domain of Fibrobacter succinogenes endoglucanase F
Author(s) -
Mitsumori Makoto,
Minato Hajime
Publication year - 2000
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.1574-6968.2000.tb08940.x
Subject(s) - clostridium thermocellum , cellulase , fibrobacter succinogenes , recombinant dna , escherichia coli , biochemistry , cellulose , hydrolase , glycoside hydrolase , peptide sequence , chemistry , structural similarity , biology , gene , enzyme , fermentation , rumen
The cellulose‐binding domain (CBD) of Fibrobacter succinogenes endoglucanase F (EGF) has been determined. The gene encoding EGF ( celF ) and its derivatives were expressed in Escherichia coli . We were able to obtain eight recombinant proteins and examine their cellulose‐binding ability and endoglucanase activity. Because four recombinant proteins, which contain the first N‐terminal reiterated region of EGF, bound to cellulose, the region has been identified as the CBD. Although the CBD did not show significant sequence similarity with any other CBDs, it did show significant similarity with a part of endoglucanase J (CelJ) of Clostridium thermocellum F1. Moreover, a large part of the C‐terminal catalytic region of EGF showed sequence similarity with α‐ L ‐arabinofuranosidases of glycosyl hydrolase family 51.