Cloning,expression and characterization of a novel acidic xylanase,XYL11B,from the acidophilic fungus Bispora sp. MEY-1 |
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Authors: | Huiying Luo Yaru Wang Jiang Li Hui wang Jun Yang Yuhui Yang Huoqing Huang Yunliu Fan Bin Yao |
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Institution: | 1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China;2. Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China;3. Department of Biology, East China Institute of Technology, Fuzhou, Jiangxi 344000, PR China |
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Abstract: | A xylanase gene (xyl11B) was cloned from Bispora sp. MEY-1 and expressed in Pichia pastoris. xyl11B, with a 66-bp intron, encodes a mature protein of 219 residues with highest identity (57.1%) to the Trichoderma reesei xylanase of glycoside hydrolase family 11. The purified recombinant XYL11B was acidophilic, exhibiting maximum activity at pH 2.6 and 65 °C. The enzyme was also thermostable, pH stable, and was highly resistant to both pepsin and trypsin, suggesting good performance in the digestive tract as a feed supplement to improve animal nutrition. The activity of XYL11B was enhanced by most metal ions but was inhibited weakly by Hg2+, Pb2+and Cu2+, which strongly inhibit many other xylanases. The specific activity of XYL11B for oat spelt xylan substrate was 2049 U mg?1. The main hydrolysis products of xylan were xylose and xylobiose. |
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