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

• Published in: World journal of microbiology & biotechnology Vol. 27; no. 2; pp. 207 - 213
• Main Authors: Wang, Jianshe, Bai, Yingguo, Shi, Pengjun, Luo, Huiying, Huang, Huoqing, Yin, Jun, Yao, Bin
• Format: Journal Article
• Language: English
• Published: Dordrecht Dordrecht : Springer Netherlands 01.02.2011; Springer Netherlands; Springer; Springer Nature B.V
• Subjects: Alicyclobacillus sp. A4; Amino acids; Applied Microbiology; Barley; Biochemistry; Biological and medical sciences; Biomedical and Life Sciences; Biotechnology; Breweries; Cloning; E coli; Environmental Engineering/Biotechnology; Enzymes; Escherichia coli; Filters; Filtration; Filtration rate; Fundamental and applied biological sciences. Psychology; Genomes; Life Sciences; mash; Microbiology; Original Paper; Peptides; pH stability; Plasmids; Proteins; Studies; Triticum aestivum; Viscosity; Xylanase; China; Viscosity; pH stability; Xylanase; Filtration rate; Mash; sp. A4; Filtration; Stability; Enzyme; Alicyclobacillus sp. A4; Brewing; Endo-1,4-β-xylanase; Glycosylases; Industry; Glycosidases; pH; Hydrolases; Xylan endo-1,3-β-xylosidase; Application
• ISSN: 0959-3993; 1573-0972
• DOI: 10.1007/s11274-010-0445-0

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.