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重组甘蔗ACC氧化酶cDNA原核表达的纯化复性研究

Purification and renaturation of recombinant sugarcane ACC oxidase expressed in Escherichia coli

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【Author】 WEI Bo~1,WANG Aiqin~(1,2),FAN Yegeng~1,WEI Yutuo~3,HE Longfei~1,YANG Litao~(1,2),Li Yangrui~4 (1 College of Agriculture,Guangxi University,Nanning 530005,China;2 Institute of Sugarcane Research,Sugar Industry Center,Guangxi University,Nanning 530004,China;3 College of Life Science and Technology,Guangxi University,Nanning 530005,China;4 Guangxi Crops Genetic Improvement Biotechnology Key Laboratory,Guangxi Academy of Agricultural Sciences,Nanning 530007,China)

【机构】广西大学农学院；广西大学生命科学与技术学院；广西作物遗传改良生物技术重点开放实验室广西南宁530005；广西南宁530005；广西大学糖业工程技术研究中心甘蔗研究所；广西南宁530004；广西南宁530007；

【摘要】重组甘蔗ACC氧化酶基因在大肠杆菌中表达,其产物以不溶性包涵体存在。用N i2+-NTA亲和层析柱对其进行纯化,结果显示,在层析柱上直接复性及纯化的方法比在变性条件下N i2+-NTA纯化然后稀释透析进行复性的方法简捷,效果好,获得的目的蛋白质纯度大于98%,活性为132.58 nm o l C2H4/(m g.h)。更多还原

【Abstract】 Recombinant sugarcane ACC oxidase gene was expressed in Escherichia coli BL21（DE3）plysS,and the product was insoluble inclusion bodies.The recombinant proteins were purified with Ni²⁺-NTA column affinity chromatography.The results showed that the approach for one-step renaturation and purification via Ni²⁺-NTA column was simpler but better than that for renaturation via dilution and dialysis the denatured protein that had been purified with Ni²⁺-NTA.The purity of the target protein obtained from one-step renaturation and purification via Ni²⁺-NTA column was higher than 98% with the specific activity 132.58 nmol C₂H₄/（mg·h）.更多还原

【关键词】重组甘蔗ACC氧化酶；融合蛋白；包涵体； Ni2+-NTA；纯化；复性；
【Key words】 recombinant sugarcane ACC oxidase； fusion protein； inclusion body； Ni²⁺-NTA； purification； renaturation；

【基金】广西科学基金(桂科青0640003);广西农业科学院博士后启动基金;广西大学博士启动基金资助

【文献出处】广西农业生物科学 ,Journal of Guangxi Agricultural and Biological Science , 编辑部邮箱 ,2006年03期

【分类号】S566.1;Q943.2
【被引频次】1
【下载频次】128

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