| 华绍烽,范云场,张磊.甲烷单加氧酶活性化合物的体外重构[J].分子催化,2016,30(6):594-598 |
| 甲烷单加氧酶活性化合物的体外重构 |
| Reconstitution of an active methane monooxygenase complex from the recombination subunits in vitro |
| 投稿时间：2016-10-21 修订日期：2016-12-16 |
| DOI： |
| 中文关键词: 甲烷单加氧酶 表达 重构 活性化合物 |
| 英文关键词:methane monooxygenase expression reconstitution active complex |
| 基金项目: |
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| 摘要点击次数: 1173 |
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| 中文摘要: |
| 甲烷氧化菌中甲烷单加氧酶既能催化甲烷转化为甲醇，也能降解小分子含氯有机物。将甲烷单加氧酶组分进行基因重组表达，利用表达的组分重构酶活性化合物，测定了重构化合物的丙烯环氧化活性及对三氯乙烯和三氯甲烷的降解。结果显示：经过30℃、220 r/min、20 min降解，约有52%的三氯乙烯被降解；在32 ℃、220 r/min、8 h反应条件下，约有26%的三氯甲烷被降解；表明甲烷单加氧酶亚基组分表达正确，能够在微生物体外重构活性化合物。 |
| 英文摘要: |
| Methanotrophs uses a soluble methane monooxygenase (sMMO) to catalyse the convertible of methane to methanol and to degrade micro-molecular organics containing chlorine. The present study describes the reconstitude sMMO complexes from individually expressed components of sMMO in Escherichia coli. functional activity of the recondtituted sMMO complexes was measured by the propylene epoxidation reaction. The TCE and chloroform degradation results were obtained with the reconstituted enzyme complex. These results demonstrate that sMMO components express correctly in Escherichia coli, biologically active complexes can be prepared by the recombinant subunits of sMMO, the degradation rate of TCE is about 52% at 30℃ for 20min at 220 r/min，for comparison, the extent of trichloromethane degradation in the recondtituted sMMO complexes is 26% in 8h at 32 ℃. |
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