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- Title
Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp.
- Authors
Lee, Charles C; Smith, Michael; Kibblewhite-Accinelli, Rena E; Williams, Tina G; Wagschal, Kurt; Robertson, George H; Wong, Dominic W S
- 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 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.
- Publication
Current microbiology, 2006, Vol 52, Issue 2, p112
- ISSN
0343-8651
- Publication type
Journal Article
- DOI
10.1007/s00284-005-4583-9