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甲氰菊酯降解酶的部分纯化及其性质研究
引用本文:林淦,黄升谋. 甲氰菊酯降解酶的部分纯化及其性质研究[J]. 河南农业科学, 2005, 0(12): 47-50
作者姓名:林淦  黄升谋
作者单位:襄樊学院化学与生物科学系,湖北,襄樊,441053
基金项目:襄樊学院科学研究基金项目(KJ04043)
摘    要:恶臭假单胞菌CP-1可以在甲氰菊酯作为碳、氮源的无机盐培养基上生长,培养60 h时,可以产生最大量的甲氰菊酯降解酶,降解酶活力达到约7.5 U/ml。该酶通过离子交换柱层析,纯化了5.67倍,比活力达到85.0U/mg,回收率为90.6%。经SDS-PAGE凝胶电泳,酶蛋白染色呈现一条主带,该酶的分子量约为78kD。等电聚焦测得酶的等电点约为6.5。冻干后的酶保存于4℃冰箱1个月,对甲氰菊酯的降解活力为原有活力的63%。

关 键 词:恶臭假单胞菌  甲氰菊酯降解酶  纯化
文章编号:1004-3268(2005)12-0047-04
收稿时间:2005-07-25
修稿时间:2005-07-25

Studies on Partial Purification of Fenpropathrin Degrading Enzyme and Its Characterization
LIN Gan,HUANG Sheng-mou. Studies on Partial Purification of Fenpropathrin Degrading Enzyme and Its Characterization[J]. Journal of Henan Agricultural Sciences, 2005, 0(12): 47-50
Authors:LIN Gan  HUANG Sheng-mou
Affiliation:Department of Chemistry and Biascience, Xiangfan University, Xiangfan 441053, China
Abstract:After cultivation for 60h in the inorganic salt medium with fenpropathrin as sole carbon and nitrogen source,Pseudomonas putida CP-1 could produce fenpropathrin-degrading enzyme in largest amounts.The vigor of degrading enzyme attained 7.5 U/ml.The enzyme was partially purified by the ion exchange,DEAE-cellulose 52 and CM-cellulose 52 chromatography,with 5.67 times purification and 90.6% recovery.The enzyme attained the specific activity of 85.0U/mg.With SDS-PAGE electrophoresis,the protein presented as a dark band.Compared with the protein marker,the molecular weight of the enzyme was roughly 78kD.The IEF-PAGE measurement showed pI of the enzyme was 6.5.The enzyme had 63% of the total degradation activity after one month restoration at 4℃.
Keywords:Pseudomonas putida  Fenpropathrin-degrading enzyme  Purification
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