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- W3147701223 abstract "A xylanase gene, xynE2, was cloned from ther- moalkaline Anoxybacillus sp. E2 and was expressed in Escherichia coli BL21 (DE3). The gene consisted of 987 bp and encoded a 328-residue xylanase with a calculated molecular weight of 38.8 kDa. On the basis of amino acid sequence similarities, this enzyme was assigned as a member of glycoside hydrolase family 10. Purified recombinant XynE2 showed maximal activity at pH 7.8 and 65C, and was thermostable at 60C. The enzyme was highly active and stable over a broad pH range, showing more than 90% of maximal activity at pH 6.6-pH 8.6 and retaining more than 80% of activity at pH 4.6-pH 12.0, 37C for 1 h, respec- tively. These favorable properties make XynE2 a good candidate in the pulp and paper industries. This is the first report on gene cloning, expression and characterization of a xylanase from the genus Anoxybacillus." @default.
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- W3147701223 date "2010-01-01" @default.
- W3147701223 modified "2023-09-23" @default.
- W3147701223 title "A new xylanase from thermoalkaline Anoxybacillus sp. E2 with high activity and stability over a broad pH range" @default.
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