Isolation and characterization of a cold-active xylanase enzyme from Flavobacterium sp.
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.
Lee
Charles C
CC
United States Department of Agriculture, Agricultural Research Service, Western Regional Research Center, 800 Buchanan St., Albany, CA 94710, USA. clee@pw.usda.gov
Smith
Michael
M
Kibblewhite-Accinelli
Rena E
RE
Williams
Tina G
TG
Wagschal
Kurt
K
Robertson
George H
GH
Wong
Dominic W S
DW
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D043364:Endo-1,4-beta Xylanases / Q000235:genetics / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology* / Q000302:isolation & purification; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D012988:Soil Microbiology; D013696:Temperature
D001426:Bacterial Proteins; D043364:Endo-1,4-beta Xylanases