Open AccessThe nature of the cellulose‐binding domain effects the activities of a bacterial endoglucanase on different forms of cellulose
Author(s) -
Coutinho J.B.,
Gilkes N.R.,
Kilburn D.G.,
Warren R.A.J.,
Miller R.C.
Publication year - 1993
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.1574-6968.1993.tb06516.x
Subject(s) - cellulase , cellulose , microcrystalline cellulose , chemistry , carboxymethyl cellulose , linker , biochemistry , enzyme , bacterial cellulose , phosphoric acid , organic chemistry , computer science , operating system , sodium
Abstract The cellulose‐binding domain (CBD CenC ) of endoglucanase C (CenC) from Cellulomonas fimi binds to amorphous (phosphoric acid‐swollen) cellulose (PASC) but not to bacterial microcrystalline cellulose (BMCC), whereas that of endoglucanase A (CBD CenA ) binds to both forms of cellulose. Substitution of CBD CenC for CBD CenA in endoglucanase A (CenA) affects the activity of the enzyme on different forms of cellulose. The hybrid enzyme (CenC″A) is less active than CenA on BMCC and Avicel. The two forms of the enzyme have similar activity on PASC. CenC″A is more active than CenA on cellulose azure and carboxymethyl cellulose. CenC″A binds to phosphoric acid‐swollen cellulose but not to crystalline cellulose. The hybrid enzyme is less sensitive than CenA to C. fimi protease, probably as a consequence of replacement of the prolyl‐threonyl linker of CenA by a triprolyl linker from CenC.