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Cloning of Bacillus licheniformis Xylanase Gene and Characterization of Recombinant Enzyme

Author:
Lee, Charles C., Kibblewhite-Accinelli, Rena E., Smith, Michael R., Wagschal, Kurt, Orts, William J., Wong, Dominic W. S.
Source:
Current microbiology 2008 v.57 no.4 pp. 301
ISSN:
0343-8651
Subject:
Bacillus licheniformis, endo-1,4-beta-xylanase, genes, molecular cloning, gene expression, Escherichia coli, enzyme activity, enzyme kinetics, enzymatic hydrolysis, xylan, thermal stability, thermophilic bacteria
Abstract:
Hemicellulose is a major component of lignocellulose biomass. Complete degradation of this substrate requires several different enzymatic activities, including xylanase. We isolated a strain of Bacillus licheniformis from a hot springs environment that exhibited xylanase activity. A gene encoding a 23-kDa xylanase enzyme, Xyn11, was cloned, and the recombinant protein was expressed in an Escherichia coli host and biochemically characterized. The optimum activity of the enzyme was at pH 5-7 and 40-50°C. The enzyme was stable at temperatures up to 50°C. Against birchwood xylan, the enzyme had an apparent K m of 6.7 mg/mL and V max of 379 μmol/min/mg.
Agid:
26779
Handle:
10113/26779