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Curr Microbiol. 2006 Feb;52(2):112-6. Epub 2006 Jan 31.

Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp.

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United States Department of Agriculture, Agricultural Research Service, Western Regional Research Center, 800 Buchanan St., Albany, CA 94710, USA.


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 degrees 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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