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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Bioproducts Research » Research » Publications at this Location » Publication #221744

Title: Cloning of Bacillus licheniformis xylanase gene and characterization of recombinant enzyme

item Lee, Charles
item Kibblewhite, Rena
item Smith, Michael
item Wagschal, Kurt
item Orts, William - Bill
item Wong, Dominic

Submitted to: Current Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/24/2008
Publication Date: 8/9/2008
Citation: Lee, C.C., Accinelli, R., Smith, M.R., Wagschal, K.C., Orts, W.J., Wong, D. 2008. Cloning of Bacillus licheniformis xylanase gene and characterization of recombinant enzyme. Current Microbiology. 57:301-305.

Interpretive Summary: Lignocellulosic biomass is considered a prime alternative to fossil fuels as a source for many of our fuel and chemical feedstock needs. After cellulose, hemicellulose comprises the largest fraction of biomass. Improved breakdown of hemicellulose is a key factor in maximizing biomass utilization. Hemicellulose is comprised primarily of xylan, a polymer of xylose residues. We cloned a gene that encode a xylanase enzyme which will degrade xylan. We biochemically characterized the enzyme and demonstrated it's ability to break down xylan under a variety of conditions.

Technical Abstract: Hemicellulose is a major component of lignocellulose biomass. Complete enzymatic degradation of this substrate requires several different activities, including xylanase. We isolated a strain of Bacillus licheniformis from a hot springs environment that exhibited xylanase activity. A gene encoding a xylanase enzyme, Xyn11, was cloned, and recombinant protein was expressed in an Escherichia coli host and biochemically characterized. The optimum activity of the enzyme was at pH 6 and 40-50oC. The enzyme was thermal stable up to 50oC. Against birch wood xylan, the enzyme had apparent Km of 6.7 mg/ml and Vmax of 379 micromol/min/mg.