Extremophiles

, Volume 10, Issue 4, pp 295–300

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

  • Charles C. Lee
  • Rena E. Kibblewhite-Accinelli
  • Kurt Wagschal
  • George H. Robertson
  • Dominic W. S. Wong
Original Paper

DOI: 10.1007/s00792-005-0499-3

Cite this article as:
Lee, C.C., Kibblewhite-Accinelli, R.E., Wagschal, K. et al. Extremophiles (2006) 10: 295. doi:10.1007/s00792-005-0499-3

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°C on native xylan substrate, and retained significant activity at lower temperatures. At 4°C, the apparent Km was 3.7 mg/ml, and the apparent kcat was 123/s.

Keywords

Xylanase Cold active Thermolabile 

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • Charles C. Lee
    • 1
  • Rena E. Kibblewhite-Accinelli
    • 1
  • Kurt Wagschal
    • 1
  • George H. Robertson
    • 1
  • Dominic W. S. Wong
    • 1
  1. 1.USDA-ARS-WRRCAlbanyUSA

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