| 刺芹侧耳多功能过氧化物酶的纯化与鉴定 |
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| 引用本文： | 陈敏,姚善泾,张虹,梁新乐.刺芹侧耳多功能过氧化物酶的纯化与鉴定[J].中国化学工程学报,2010,18(5):824-829. |
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| 作者姓名： | 陈敏 姚善泾 张虹 梁新乐 |
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| 作者单位： | 1. Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027, China;2. Department of Biotechnology Engineering, Zhejiang Gongshang University, Hangzhou 310012, China |
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| 基金项目： | Supported by the Special Funds for Major State Basic Research Program of China (2007CB707805);the Natural Science Foundation of Zhejiang Province (Y505334) |
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| 摘 要： | A versatile peroxidase (VP-Peco60-7) was generated and purified from the liquid culture of Pleurotus eryngii. The purification procedure included ammonium sulfate precipitation, ion exchange chromatography, and gel chromatography. The molecular weight and isoelectric point (pI) of VP-Peco60-7 were determined to be approximately 40 kDa and 4.1, respectively. By N-terminal sequence determination and peptide mapping analysis, VP-Peco60-7 was found to be similar to the versatile peroxidase isoenzyme VPL1, which was previously isolated from liquid cultures of the same species. However, the molecular weight and pI of VP-Peco60-7 were different from those of versatile peroxidases of liquid cultures, implying that the VP-Peco60-7 in this study is of a novel type. With 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) as a substrate, the maximal enzyme activity was obtained at 50 °C and pH 3.0. The catalysis of ABTS by VP-Peco60-7 was expressed by the Michaelis-Menten equation. At 50 °C and pH 3.0, the maxi-mum velocity (Vmax) was 188.68 U•mg1 and the michaelis constant (Km) was 203.09 mmol•L1.
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| 关 键 词： | Pleurotus eryngii versatile peroxidase purification enzymatic properties |
| 收稿时间： | 2009-12-29 |
| 修稿时间： | 2009-12-29
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Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii |
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| CHEN Min,YAO Shanjing,ZHANG Hong,LIANG Xinle.Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii[J].Chinese Journal of Chemical Engineering,2010,18(5):824-829. |
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| Authors: | CHEN Min YAO Shanjing ZHANG Hong LIANG Xinle |
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| Affiliation: | 1. Department of Chemical and Biochemical Engineering, Zhejiang University, Hangzhou 310027, China;2. Department of Biotechnology Engineering, Zhejiang Gongshang University, Hangzhou 310012, China |
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| Abstract: | A versatile peroxidase (VP-Peco60-7) was generated and purified from the liquid culture of Pleurotus eryngii. The purification procedure included ammonium sulfate precipitation, ion exchange chromatography, and gel chromatography. The molecular weight and isoelectric point (pI) of VP-Peco60-7 were determined to be approxi-mately 40 kDa and 4.1, respectively. By N-terminal sequence determination and peptide mapping analysis, VP-Peco60-7 was found to be similar to the versatile peroxidase isoenzyme VPL1, which was previously isolated from liquid cultures of the same species. However, the molecular weight and pI of VP-Peco60-7 were different from those of versatile peroxidases of liquid cultures, implying that the VP-Peco60-7 in this study is of a novel type. With 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) as a substrate, the maximal enzyme activity was obtained at 50℃ and pH 3.0. The catalysis of ABTS by VP-Peco60-7 was expressed by the Michaelis-Menten equa-tion. At 50℃ and pH 3.0, the maximum velocity (Vmax) was 188.68 U·mg-1 and the michaelis constant (Km) was 203.09 μmol·L-1. |
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| Keywords: | Pleurotus eryngii versatile peroxidase purification enzymatic properties |
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