Characterization of A Recombinant Thermostable Xylanase from Hot Spring Thermophilic Geobacillus sp. TC-W7
A xylanase-producing thermophilic strain Geobacillus sp.TC-W7, was isolated from a hot spring in Yongtai (Fuzhou, China). Subsequently, the xylanase gene that encoded 407 amino acids was cloned and expressed. The recombinant xylanase was purified by GST affinity chromatography and exhibited maximum activity at 75°C and a pH of 8.2. The enzyme was active up to 95°C and showed activity over a wide pH range from 5.2 to 10.2. Additionally, the recombinant xylanase showed high thermostability and pH stability. More than 85％ of the enzyme’s activities were retained after incubations at 70°C for 90 min at a pH of 8.2. The activity of the recombinant xylanase was enhanced by treatment with 10 mM enzyme inhibitors (DDT, Tween-20, 2-Me or TritonX-100) and was inhibited by EDTA or PMSF. Its functionality was stable in the presence of Li+, Na+ and K+, but inhibited by Hg2+, Ni2+, Co2+, Cu2+, Zn2+, Pb2+, Fe3+ and Al3+. The functionality of the crude xylanase had similar properties to the recombinant xylanase except for when it was treated with Al2+ or Fe2+. The enzyme might be a promising candidate for various industrial applications such as biofuel, food, paper and the pulp industry.
Thermostable xylanase Recombinant expression Characterization Stable pH Geobacillus sp. TC-W7
Bin Liu Ningning Zhang Chao Zhao Baixue Lin Lianhui Xie Yifan Huang
Institute of Bioenergy, College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Institute of Bioenergy, Institute of Plant Virology College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China Na
国内会议
福州
英文
152-161
2012-07-12（万方平台首次上网日期，不代表论文的发表时间）