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

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Abstract

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 55°C. The enzyme was stable over a broad pH range, retaining more than 90% of the original activity at pH 5.8–12.0, 37°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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Acknowledgments

This work was supported by the National High Technology Research and Development Program of China (863 program, grant 2007AA100601) and Agricultural Science and Technology Conversion Funds (grant 2008GB23260388) and the Earmarked Fund for Modern Agro-industry Technology Research System (NYCYTX-42-G2-05).

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Authors and Affiliations

  1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, 100081, Beijing, People’s Republic of China

    Jianshe Wang, Yingguo Bai, Pengjun Shi, Huiying Luo, Huoqing Huang & Bin Yao

  2. College of Life Sciences, Inner Mongolia Agricultural University, 010018, Hohhot, People’s Republic of China

    Jianshe Wang & Jun Yin

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  1. Jianshe Wang
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  2. Yingguo Bai
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  3. Pengjun Shi
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  4. Huiying Luo
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  5. Huoqing Huang
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  6. Jun Yin
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  7. Bin Yao
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Correspondence to Bin Yao.

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Wang, J., Bai, Y., Shi, P. et al. A novel xylanase, XynA4-2, from thermoacidophilic Alicyclobacillus sp. A4 with potential applications in the brewing industry. World J Microbiol Biotechnol 27, 207–213 (2011). https://doi.org/10.1007/s11274-010-0445-0

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