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

Lee, Charles; Kibblewhite-Accinelli, Rena; Wagschal, Kurt; Robertson, George; Wong, Dominic

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 K m was 3.7 mg/ml, and the apparent k cat was 123/s.

XYLANASES; AMINO acids; CLONING; MOLECULAR weights; INDUSTRIAL enzymology; BIOCHEMICAL engineering

Extremophiles, 2006, Vol 10, Issue 4, p295

1431-0651

Academic Journal

10.1007/s00792-005-0499-3