A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability.

Journal of Industrial Microbiology & Biotechnology
Yingguo BaiBin Yao

Abstract

We have identified a highly pH-adaptable and stable xylanase (XynA4) from the thermoacidophilic Alicyclobacillus sp. A4, a strain that was isolated from a hot spring in Yunnan Province, China. The gene (xynA4) that encodes this xylanase was cloned, sequenced, and expressed in Escherichia coli. It encodes a 338-residue polypeptide with a calculated molecular mass of 42.5 kDa. The deduced amino acid sequence is most similar to (53% identity) an endo-1,4-beta-xylanase from Geobacillus stearothermophilus that belongs to family 10 of the glycoside hydrolases. Purified recombinant XynA4 exhibited maximum activity at 55 degrees C and pH 7.0, had broad pH adaptability (>40% activity at pH 3.8-9.4) and stability (retaining >80% activity after incubation at pH 2.6-12.0 for 1 h at 37 degrees C), and was highly thermostable (retaining >90% activity after incubation at 60 degrees C for 1 h at pH 7.0). These properties make XynA4 promising for application in the paper industry. This is the first report that describes cloning and expression of a xylanase gene from the genus Alicyclobacillus.

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Citations

Aug 6, 2010·Journal of Industrial Microbiology & Biotechnology·Junpei ZhouBin Yao
Apr 12, 2011·Journal of Industrial Microbiology & Biotechnology·Indira P SarethySanjay Gupta
Nov 7, 2015·Journal of Industrial Microbiology & Biotechnology·John E AstonVicki S Thompson
Jul 29, 2015·Enzyme and Microbial Technology·Beatrice Cobucci-PonzanoMarco Moracci
Apr 15, 2014·Bioresource Technology·Aditya BhallaRajesh K Sani

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