A novel xylanase, XynA4-2, from thermoacidophilic Alicyclobacillus sp A4 with potential applications in the brewing industry

文献类型： 外文期刊

第一作者： Wang, Jianshe

作者： Wang, Jianshe;Bai, Yingguo;Shi, Pengjun;Luo, Huiying;Huang, Huoqing;Yao, Bin;Wang, Jianshe;Yin, Jun

作者机构：

关键词： Alicyclobacillus sp A4;Xylanase;pH stability;Mash;Viscosity;Filtration rate

期刊名称：WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY （ 影响因子：3.312； 五年影响因子：3.58 ）

ISSN： 0959-3993

年卷期： 2011 年 27 卷 2 期

页码：

收录情况： SCI

摘要： A xylanase gene, xynA4-2, was obtained from the genome sequence of thermoacidophilic Alicyclobacillus sp. A4 and expressed in Escherichia coli BL21 (DE3). xynA4-2 encodes a mature protein of 411 residues with a calculated molecular weight of 46.8 kDa. Based on the amino acid sequence similarities (highest identity of 61%), the enzyme was confined into glycoside hydrolase family 10. The purified recombinant XynA4-2 exhibited maximum activity at pH 6.2 and 55A degrees C. The enzyme was stable over a broad pH range, retaining more than 90% of the original activity at pH 5.8-12.0, 37A degrees C for 1 h. The substrate specificity of XynA4-2 was relatively narrow, exhibiting 100, 93, and 35% of the relative activity towards birchwood xylan, oat spelt xylan, and wheat arabinoxylan, respectively. Supplementation of XynA4-2 to mash caused the reduction of mash filtration rate (5.6%) and viscosity (4.0%). When combined with the commercial glucanase from Sunson, higher reduction was detected in the filtration rate (12.0%) and viscosity (17.2%). These favorable properties make XynA4-2 a good candidate in the brewing industry.

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