| 重组产几丁质酶C工程菌包涵体的复性 |
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| 引用本文： | 蔡婀娜,贺淹才,刘治江,李红然.重组产几丁质酶C工程菌包涵体的复性[J].河南师范大学学报(自然科学版),2011,39(1):137-141. |
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| 作者姓名： | 蔡婀娜 贺淹才 刘治江 李红然 |
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| 作者单位： | 华侨大学,化工学院生物工程系,福建,泉州,362021 |
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| 摘 要： | 将重组产几丁质酶C(Chi C)的菌体通过固定金属鳌合层析(IMAC),对目的蛋白进行初步纯化;然后采用透析法、凝胶过滤柱层析法和金属鳌合柱层析法对包涵体进行复性.结果表明,逐渐降低变性剂尿素浓度进行透析复性,酶液的酶活力为58.85 μkat·L-1,比活为0.425 mkat·g-1,蛋白回收率为95.3%.使用S...
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| 关 键 词： | 几丁质酶 C 包涵体 复性 透析法 凝胶过滤柱层析法 金属螯合层析法 |
Comparison of Three Renaturation for the Inclusion Bodies of the Recombinant Chitinase C Producing Engineering Bacteria |
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| CAI E-na,HE Yan-cai,LIU Zhi-jiang,LI Hong-ran.Comparison of Three Renaturation for the Inclusion Bodies of the Recombinant Chitinase C Producing Engineering Bacteria[J].Journal of Henan Normal University(Natural Science),2011,39(1):137-141. |
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| Authors: | CAI E-na HE Yan-cai LIU Zhi-jiang LI Hong-ran |
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| Institution: | (College of Chemical Engineering,Huaqiao Univeisity,Quanzhou 362021,China) |
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| Abstract: | The recombinant proteins of the Recombinant Chitinase C Producing Escherichia coli are purified by passing through immobilized metal affinity chromatography(IMAC),these inclusion bodies are renaturated by three Methods-membrane dialysis,gel filtration chromatography and IMAC.The results are :(1) renaturated by gradually decreasing the urea concentration dialysis,the enzyme activity is 58.85 μkat·L-1,the specific activity is 0.425 mkat·g-1,and the protein recovery rate is 95.3%;(2)renaturated by SepHacry S-200 gel filtration chromatography,the enzyme activity is 30.37μkat·L-1,the specific activity is 0.620 mkat·g-1,and the protein recovery rate is 72.9%;(3)renaturated by IMAC,the enzyme activity is 55.59 μkat·L-1,the specific activity is 1.917 mkat·g-1,and the protein recovery rate is 43.2%. |
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| Keywords: | Chitinase C inclusion body renaturation gel filtration chromatography metal affinity chromatography |
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