Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii
Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii作者机构：Department of Chemical and Biochemical Engineering Zhejiang University Hangzhou 310027 China Deigartment of Biotechnology Engineering Zhejiang Gongshang University Hangzhou 310012 China
出 版 物：《Chinese Journal of Chemical Engineering》 (中国化学工程学报（英文版）)
年 卷 期：2010年第18卷第5期
页 面：824-829页
核心收录：
学科分类：09[农学] 0901[农学-作物学] 0902[农学-园艺学] 090202[农学-蔬菜学]
基 金：Supported by the Special Funds for Major State Basic Research Program of China (2007CB707805) the Natural Science Foundation of Zhejiang Province (Y505334)
主 题：Pleurotus eryngii versatile peroxidase purification enzymatic properties
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 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 °C and pH 3.0. The catalysis of ABTS by VP-Peco60-7 was expressed by the Michaelis-Menten equa-tion. At 50 °C and pH 3.0, the maximum velocity (V max ) was 188.68 U·mg-1 and the michaelis constant (K m ) was 203.09 μmol·L-1 .
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