Title |
Cloning and Characterization of the Xyn11A Gene from Lentinula edodes
|
---|---|
Published in |
The Protein Journal, January 2005
|
DOI | 10.1007/s10930-004-0602-0 |
Pubmed ID | |
Authors |
Charles C. Lee, Dominic W. S. Wong, George H. Robertson |
Abstract |
Hemicellulose represents a rich source of biomass that can be converted into useful chemical feedstocks. One of the main components of hemicellulose is xylan, a polymer of xylose residues. Xylanase enzymes that hydrolyze xylan are therefore of great commercial interest. We have cloned a gene (xyn11A) that encodes a 283-amino acid xylanase enzyme from the fungus Lentinula edodes. The enzyme has a pI of 4.6 and belongs to the highly conserved glycosyl hydrolase family 11. The xylanase gene was cloned into a Pichia pastoris expression vector that secretes active enzyme into both solid and liquid media. The optimal reaction conditions were at pH 4.5 and 50 degrees C. The enzyme had a Km of 1.5 mg/ml and a Vmax of 2.1 mmol/min/mg. Xyn11A produced primarily xylobiose, xylotriose, and xylotetraose from a birchwood xylan substrate. This is the first report on the cloning of a hemicellulase gene from L. edodes. |
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