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耐冷皮壳正青霉一种木聚糖酶的纯化与性质研究
引用本文: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.
作者姓名:朱会芳  周鹏  闫巧娟  江正强
作者单位:1. 中国农业大学食品科学与营养工程学院,北京,100083
2. 中国农业大学工学院,北京,100083
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)
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pH4.5-6.5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。

关 键 词:木聚糖酶  低温  真菌  酶学性质

Purification and characterization of a xylanase from psychrotrophic Eupenicillium crustaceum
Authors:ZHU Hui-Fang  ZHOU Peng  YAN Qiao-Juan and JIANG Zheng-Qiang
Institution:College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China;College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China;College of Engineering, China Agricultural University, Beijing 100083, China;College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China
Abstract: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.
Keywords:xylanase  low temperature  fungi  enzymatic characterization
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