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Extremophiles. 2006 Aug;10(4):295-300. Epub 2006 Mar 11.

Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library.

Author information

  • 1USDA-ARS-WRRC, 800 Buchanan St., Albany, CA 94710, USA. clee@pw.usda.gov

Abstract

There is a great interest in xylanases due to the wide variety of industrial applications for these enzymes. We cloned a xylanase gene (xyn8) from an environmental genomic DNA library. The encoded enzyme was predicted to be 399 amino acids with a molecular weight of 45.9 kD. The enzyme was categorized as a glycosyl hydrolase family 8 member based on sequence analysis of the putative catalytic domain. The purified enzyme was thermolabile, had an activity temperature optimum of 20 degrees C on native xylan substrate, and retained significant activity at lower temperatures. At 4 degrees C, the apparent K (m) was 3.7 mg/ml, and the apparent k (cat) was 123/s.

PMID:
16532363
DOI:
10.1007/s00792-005-0499-3
[PubMed - indexed for MEDLINE]
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