Browse by author
Lookup NU author(s): Emeritus Professor Harry Gilbert
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Xylanase Xyn10B from Clostridium thermocellum is a modular enzyme that contains two family 22 carbohydrate binding modules N- (CBM22-1) and C- (CBM22-2) terminal of the family 10 glycoside hydrolase catalytic domain (GH10). In a previous study, we showed that removal of CBM22-1 reduces the resistance to thermoinactivation of the enzyme suggesting that this module is a thermo stabilizing domain. Here, we show that it is the module border on the N-terminal side of GH10 that confers resistance to thermoinactivation and to proteolysis. Therefore, CBM22-1 does not function as a thermostabilizing domain and the role for this apparently non-functional CBM remains elusive. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Author(s): Dias FMV, Goyal A, Gilbert HJ, Prates JAM, Ferreira LMA, Fontes CMGA
Publication type: Article
Publication status: Published
Journal: FEMS Microbiology Letters
ISSN (print): 0378-1097
ISSN (electronic): 1574-6968
Altmetrics provided by Altmetric