Cloning and characterization of a cold-active xylanase enzyme from an environmental DNA library
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- Lee, C.C., Kibblewhite-Accinelli, R.E., Wagschal, K. et al. Extremophiles (2006) 10: 295. doi:10.1007/s00792-005-0499-3
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.