Abstract
A xylanase gene (xyn10A) was cloned from Bacillus sp. SN5 and expressed in Escherichia coli. It encoded a 348-residue polypeptide of ~45kDa. The deduced amino acid sequence had 68% identity with the endo-1,4-beta-xylanase from Paenibacillus lactis 154 that belonged to family 10 of the glycoside hydrolases. Purified recombinant Xyn10A had maximum activity at 40°C and pH 7.0, with the specific activity of 105U/mg and a Km of 0.6mg/ml for beechwood xylan. Xyn10A retained more than 80% activity between 25 and 45°C and 29% activity at 5°C. It exhibited the highest activity (134%) in 0.5M NaCl and still retained 90% activity in 2.5M NaCl. It retained about 87% activity after incubation in 2M NaCl for 24h. The cold-active and halo-tolerant properties of Xyn10A make it promising for application in the food industry, especially in the processing of saline food and sea food.
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