Open AccessThe modular cellulase CelZ of the thermophilic bacterium Clostridium stercorarium contains a thermostabilizing domain
Author(s) -
Riedel Kathrin,
Ritter Johannes,
Bauer Stefan,
Bronnenmeier Karin
Publication year - 1998
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.1574-6968.1998.tb13096.x
Subject(s) - cellulase , thermostability , thermophile , cellulose , enzyme , chemistry , domain (mathematical analysis) , biochemistry , clostridium thermocellum , biology , mathematics , mathematical analysis
The non‐catalytic region of the Clostridium stercorarium cellulase CelZ (Avicelase I) comprises two protein segments (C and C′) grouped into different subfamilies of cellulose‐binding domain (CBD) family III. The C‐terminally located family IIIb domain C was identified as a true cellulose‐binding domain responsible for anchoring the CelZ enzyme to cellulose. The family IIIc domain C′ immediately adjacent to the catalytic domain was unable to mediate binding to cellulose. A deletion study revealed a lack of independence of this pair of domains: almost the entire C′ domain was required to maintain the catalytic activity and the thermostability of the enzyme.