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

被引：48

作者：

Lee, CC ^{[1
]}

Smith, M ^{[1
]}

Kibblewhite-Accinelli, R ^{[1
]}

Williams, TG ^{[1
]}

Wagschal, K ^{[1
]}

Robertson, GH ^{[1
]}

Wong, DWS ^{[1
]}

机构：

[1] USDA, ARS, Western Reg Res Ctr, Albany, CA 94710 USA

来源：

CURRENT MICROBIOLOGY | 2006年 / 52卷 / 02期

关键词：

D O I：

10.1007/s00284-005-4583-9

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 K-m of 1.8 mg/ml and k(cat) of 100 sec(-1) for beechwood xylan, attacks highly branched native xylan substrates, and does not have activity against glucans.

引用

页码：112 / 116

页数：5

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