Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii
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...
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| description | 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 . |
| doi_str_mv | 10.1016/S1004-9541(09)60134-8 |
| format | Article |
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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. 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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 .</description><subject>Chromatography</subject><subject>Culture</subject><subject>enzymatic properties</subject><subject>Liquids</subject><subject>Mathematical analysis</subject><subject>Molecular weight</subject><subject>Peroxidase</subject><subject>Pleurotus eryngii</subject><subject>Purification</subject><subject>versatile peroxidase</subject><subject>多功能</subject><subject>杏鲍菇</subject><subject>液体培养</subject><subject>离子交换层析</subject><subject>过氧化物酶同工酶</subject><subject>食用菌</subject><issn>1004-9541</issn><issn>2210-321X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNqFUVFLHDEQDqVCr-pPEJa-qA9rM0l2N_tU5LAqWDywLb6FbDK5S93baLIrtb_enCd9VBgYvuH7vmG-IeQA6AlQqL_eAKWibCsBR7Q9rilwUcoPZMYY0JIzuP1IZv8pn8jnlP5QyqgEOSPdYoreeaNHH4ZCD7aYr3TUZsTo_22HwRW6-I0xZdhjscAY_nqrExYuhnVxZn2Xxz-mtIoh40WPUwzjlAqMT8PS-z2y43SfcP-175Jf389-zi_Kq-vzy_npVWkEhbEU3AprpDGGC2071lhsbF2Daxm6XFxqDQCs463maMAhz0dJLSlQx2zFd8nh1vc-hocJ06jWPhnsez1gmJKSohUNr1iTmUdvMqFugMmG041ptaWaGFKK6NR99GsdnxRQtUlfvaSvNtEq2qqX9JXMum9bHeaLHz1GlYzHwaD1Ec2obPDvOnx53bwKw_LBD0vVaXPn8g8UrxpW17zlz9JJmPk</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>陈敏 姚善泾 张虹 梁新乐</creator><general>Elsevier B.V</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W95</scope><scope>~WA</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>M7N</scope></search><sort><creationdate>20101001</creationdate><title>Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii</title><author>陈敏 姚善泾 张虹 梁新乐</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-43d4dc8ccc34adb27de7d661f92ef2ef38aa1112b39a3ec1fe31008a8010f2d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Chromatography</topic><topic>Culture</topic><topic>enzymatic properties</topic><topic>Liquids</topic><topic>Mathematical analysis</topic><topic>Molecular weight</topic><topic>Peroxidase</topic><topic>Pleurotus eryngii</topic><topic>Purification</topic><topic>versatile peroxidase</topic><topic>多功能</topic><topic>杏鲍菇</topic><topic>液体培养</topic><topic>离子交换层析</topic><topic>过氧化物酶同工酶</topic><topic>食用菌</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>陈敏 姚善泾 张虹 梁新乐</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-农业科学</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Chinese journal of chemical engineering</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>陈敏 姚善泾 张虹 梁新乐</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii</atitle><jtitle>Chinese journal of chemical engineering</jtitle><addtitle>Chinese Journal of Chemical Engineering</addtitle><date>2010-10-01</date><risdate>2010</risdate><volume>18</volume><issue>5</issue><spage>824</spage><epage>829</epage><pages>824-829</pages><issn>1004-9541</issn><eissn>2210-321X</eissn><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 °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 .</abstract><pub>Elsevier B.V</pub><doi>10.1016/S1004-9541(09)60134-8</doi><tpages>6</tpages></addata></record> |
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| subjects | Chromatography Culture enzymatic properties Liquids Mathematical analysis Molecular weight Peroxidase Pleurotus eryngii Purification versatile peroxidase 多功能 杏鲍菇 液体培养 离子交换层析 过氧化物酶同工酶 食用菌 |
| title | Purification and Characterization of a Versatile Peroxidase from Edible Mushroom Pleurotus eryngii |
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