Editor: Dieter Jahn
Characterization of a new β-glucosidase/β-xylosidase from the gut microbiota of the termite (Reticulitermes santonensis)
Article first published online: 26 NOV 2010
FEMS Microbiology Letters © 2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. No claim to original Belgian government works
FEMS Microbiology Letters
Volume 314, Issue 2, pages 147–157, January 2011
How to Cite
Mattéotti, C., Haubruge, E., Thonart, P., Francis, F., De Pauw, E., Portetelle, D. and Vandenbol, M. (2011), Characterization of a new β-glucosidase/β-xylosidase from the gut microbiota of the termite (Reticulitermes santonensis). FEMS Microbiology Letters, 314: 147–157. doi: 10.1111/j.1574-6968.2010.02161.x
- Issue published online: 16 DEC 2010
- Article first published online: 26 NOV 2010
- Accepted manuscript online: 11 NOV 2010 12:44PM EST
- Received 11 August 2010; revised 13 October 2010; accepted 29 October 2010.Final version published online 26 November 2010.
- genomic library;
- bgl operon;
The gut of the termite Reticulitermes santonensis contains an interesting diversity of prokaryotic and eukaryotic microorganisms not found elsewhere. These microorganisms produce many enzyme-digesting lignocellulosic compounds, probably in cooperation with endogenous enzymes. Regarding cellulose and hemicellulose digestion in the termite gut, much remains to be learned about the relative contributions of termite enzymes and enzymes produced by different microorganisms. Here we grew bacterial colonies from termite gut suspensions, identifying 11 of them after PCR amplification of their 16S rRNA genes. After constructing in Escherichia coli a genomic DNA library corresponding to all of the colonies obtained, we performed functional screening for α-amylase, xylanase, β-glucosidase, and endoglucanase activities. This screen revealed a clone producing β-glucosidase activity. Sequence analysis showed that the cloned genomic DNA fragment contained three complete ORFs (bglG, bglF, and bglB) organized in a putative bgl operon. The new β-glucosidase (BglB), identified with its regulators BglG and BglF, belongs to glycoside hydrolase family 1. The new β-glucosidase was expressed in E. coli and purified by affinity chromatography. The purified enzyme shows maximal activity at pH 6.0 and 40 °C. It also displays β-xylosidase activity.