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Applied and Environmental Microbiology, February 2003, p. 869-877, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.869-877.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Production by Clostridium acetobutylicum ATCC 824 of CelG, a Cellulosomal Glycoside Hydrolase Belonging to Family 9

Ana M. López-Contreras,1,2* Aernout A. Martens,1 Nora Szijarto,2 Hans Mooibroek,2 Pieternel A. M. Claassen,2 John van der Oost,1 and Willem M. de Vos1

Laboratory of Microbiology,1 Agrotechnological Research Institute (ATO), Wageningen University and Research Centre, Wageningen, The Netherlands2

Received 17 July 2002/ Accepted 31 October 2002

The genome sequence of Clostridium acetobutylicum ATCC 824, a noncellulolytic solvent-producing strain, predicts the production of various proteins with domains typical for cellulosomal subunits. Most of the genes coding for these proteins are grouped in a cluster similar to that found in cellulolytic clostridial species, such as Clostridium cellulovorans. CAC0916, one of the open reading frames present in the putative cellulosome gene cluster, codes for CelG, a putative endoglucanase belonging to family 9, and it was cloned and overexpressed in Escherichia coli. The overproduced CelG protein was purified by making use of its high affinity for cellulose and was characterized. The biochemical properties of the purified CelG were comparable to those of other known enzymes belonging to the same family. Expression of CelG by C. acetobutylicum grown on different substrates was studied by Western blotting by using antibodies raised against the purified E. coli-produced protein. Whereas the antibodies cross-reacted with CelG-like proteins secreted by cellobiose- or cellulose-grown C. cellulovorans cultures, CelG was not detectable in extracellular medium from C. acetobutylicum grown on cellobiose or glucose. However, notably, when lichenan-grown cultures were used, several bands corresponding to CelG or CelG-like proteins were present, and there was significantly increased extracellular endoglucanase activity.

* Corresponding author. Present address: Bioconversion Group, Agrotechnological Research Institute (ATO), P. O. Box 17, 6700 AA Wageningen, The Netherlands. Phone: 31 317 478572. Fax: 31 317 475347. E-mail: a.m.lopezcontreras{at}ato.wag-ur.nl.

Applied and Environmental Microbiology, February 2003, p. 869-877, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.869-877.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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