Isolation and Characterization of a Cold-Active Xylanase Enzyme from Flavobacterium sp. |
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Authors: | Charles C Lee Michael Smith Rena E Kibblewhite-Accinelli Tina G Williams Kurt Wagschal George H Robertson Dominic W S Wong |
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Institution: | (1) United States Department of Agriculture, Agricultural Research Service, Western Regional Research Center, 800 Buchanan St., Albany, CA 94710, USA |
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Abstract: | Xylan is the major component of hemicellulose, and xylan should be fully utilized to improve the efficiencies of a biobased
economy. There are a variety of industrial reaction conditions in which an active xylanase enzyme would be desired. As a result,
xylanase enzymes with different activity profiles are of great interest. We isolated a xylanase gene (xyn10) from a Flavobacterium sp. whose sequence suggests that it is a glycosyl hydrolase family 10 member. The enzyme has a temperature optimum of 30°C,
is active at cold temperatures, and is thermolabile. The enzyme has an apparent Km of 1.8 mg/ml and kcat of 100 sec−1 for beechwood xylan, attacks highly branched native xylan substrates, and does not have activity against glucans. |
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