耐冷皮壳正青霉一种木聚糖酶的纯化与性质研究
Purification and characterization of a xylanase from psychrotrophic Eupenicillium crustaceum
  
中文关键词:木聚糖酶,低温,真菌,酶学性质
英文关键词:xylanase, low temperature, fungi, enzymatic characterization
基金项目:高等学校博士学科点专项科研基金资助课题;全国优秀博士学位论文作者专项资金(No. 200555)
作者单位
朱会芳 中国农业大学食品科学与营养工程学院 北京 100083 
周鹏 中国农业大学食品科学与营养工程学院 北京 100083 
闫巧娟 中国农业大学工学院 北京 100083 
江正强 中国农业大学食品科学与营养工程学院 北京 100083 
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中文摘要:
      研究了耐冷皮壳正青霉Eupenicillium crustaceum一种木聚糖酶的纯化和酶学性质。采用硫酸铵沉淀和阴离子交换层析的方法,从耐冷皮壳正青霉液体发酵液中分离纯化出一种亚基分子量35kDa的木聚糖酶。酶学性质研究表明,酶的最适pH值为5.5,在pH 4.5-6.5范围内具有较高的催化活性。最适温度为50℃,20℃下酶活为最高酶活的40%。Ag+和Fe2+大幅度提高木聚糖酶的酶活,而Mn2+和Hg2+强烈抑制木聚糖酶的活性。同时,该木聚糖酶具有严格的底物特异性。
英文摘要:
      A xylanase from psychrotrophic Eupenicillium crustaceum was purified and characterized. The xylanase was purified to homogeneity by ammonium precipitation and anion-exchange chromatography and its subunit molecular mass was estimated to be 35kDa by SDS-PAGE. The xylanase showed apparent optimal activity at pH 5.5 and 50℃. It retained more than 80% of its maximum activity at pH 4.5-6.5 and retainded 40% of its maximum activity at 20℃. The enzyme was greatly activated by Ag+ and Fe2+, and strongly inhibited by Mn2+ and Hg2+. The xylanase displayed a strict substrate specificity.
朱会芳,周鹏,闫巧娟,江正强. 耐冷皮壳正青霉一种木聚糖酶的纯化与性质研究[J]. 菌物学报, 2010, 29(4): 536-541
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