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

Springer Science and Business Media LLC - Tập 10 - Trang 295-300 - 2006
Charles C. Lee1, Rena E. Kibblewhite-Accinelli1, Kurt Wagschal1, George H. Robertson1, Dominic W. S. Wong1
1USDA-ARS-WRRC, Albany, USA

Tóm tắt

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.

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