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Applied and Environmental Microbiology, October 2007, p. 6098-6105, Vol. 73, No. 19
0099-2240/07/$08.00+0     doi:10.1128/AEM.01037-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Characterization and Synergistic Interactions of Fibrobacter succinogenes Glycoside Hydrolases ^,

Meng Qi, Hyun-Sik Jun, and Cecil W. Forsberg^*

Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada

Received 9 May 2007/ Accepted 21 July 2007

The objectives of this study were to characterize Fibrobacter succinogenes glycoside hydrolases from different glycoside hydrolase families and to study their synergistic interactions. The gene encoding a major endoglucanase (endoglucanase 1) of F. succinogenes S85 was identified as cel9B from the genome sequence by reference to internal amino acid sequences of the purified native enzyme. Cel9B and two other glucanases from different families, Cel5H and Cel8B, were cloned and overexpressed, and the proteins were purified and characterized. These proteins in conjunction with two predominant cellulases, Cel10A, a chloride-stimulated cellobiosidase, and Cel51A, formerly known as endoglucanase 2 (or CelF), were assayed in various combinations to assess their synergistic interactions using ball-milled cellulose. The degree of synergism ranged from 0.6 to 3.7. The two predominant endoglucanases produced by F. succinogenes, Cel9B and Cel51A, were shown to have a synergistic effect of up to 1.67. Cel10A showed little synergy in combination with Cel9B and Cel51A. Mixtures containing all the enzymes gave a higher degree of synergism than those containing two or three enzymes, which reflected the complementarity in their modes of action as well as substrate specificities.

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* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada. Phone: (519) 824-4120, ext. 53433. Fax: (519) 837-1802. E-mail: cforsber{at}uoguelph.ca

Published ahead of print on 27 July 2007.

Supplemental material for this article may be found at http://aem.asm.org/.

Present address: Section on Cellular Differentiation, NICHD, National Institutes of Health, Bldg. 10, Room 10N325, 9000 Rockville Pike, Bethesda, MD 20892.

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Applied and Environmental Microbiology, October 2007, p. 6098-6105, Vol. 73, No. 19
0099-2240/07/$08.00+0     doi:10.1128/AEM.01037-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Qi, M., Jun, H.-S., Forsberg, C. W. (2008). Cel9D, an Atypical 1,4-{beta}-D-Glucan Glucohydrolase from Fibrobacter succinogenes: Characteristics, Catalytic Residues, and Synergistic Interactions with Other Cellulases. J. Bacteriol. 190: 1976-1984 [Abstract] [Full Text]  
• Qi, M., Nelson, K. E., Daugherty, S. C., Nelson, W. C., Hance, I. R., Morrison, M., Forsberg, C. W. (2008). Genomic Differences between Fibrobacter succinogenes S85 and Fibrobacter intestinalis DR7, Identified by Suppression Subtractive Hybridization. Appl. Environ. Microbiol. 74: 987-993 [Abstract] [Full Text]