An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters
An extracellular enzyme capable of efficient hydrolysis of xanthophyll esters was purified from culture supernatants of the basidiomycete Pleurotus sapidus. Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunit...
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| Veröffentlicht in: | Biological chemistry 2005-05, Vol.386 (5), p.435-440 |
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| creator | Zorn, Holger Bouws, Henning Takenberg, Meike Nimtz, Manfred Getzlaff, Rita Breithaupt, Dietmar E. Berger, Ralf G. |
| description | An extracellular enzyme capable of efficient hydrolysis of xanthophyll esters was purified from culture supernatants of the basidiomycete Pleurotus sapidus. Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40°C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. The P. sapidus carboxylesterase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus that has been characterised at the molecular level. |
| doi_str_mv | 10.1515/BC.2005.052 |
| format | Article |
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Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40°C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. 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Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40°C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. The P. sapidus carboxylesterase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus that has been characterised at the molecular level.</description><subject>Amino Acid Sequence</subject><subject>Basidiomycetes</subject><subject>Candida rugosa</subject><subject>Carboxylic Ester Hydrolases - chemistry</subject><subject>Carboxylic Ester Hydrolases - isolation & purification</subject><subject>carotenoids</subject><subject>cDNA library</subject><subject>Esters - chemistry</subject><subject>Extracellular Fluid - enzymology</subject><subject>fungi</subject><subject>Hydrolysis</subject><subject>Isoelectric Point</subject><subject>lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - isolation & purification</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Pleurotus</subject><subject>Pleurotus - enzymology</subject><subject>Protein Conformation</subject><subject>Xanthophylls - chemistry</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EoqVw4o584oKy9WdsH9uUQqWiFqmcLceZKAFnvdiJtPn3eLsrOHKaGc2jdz5ehN5TsqGSysvrZsMIkRsi2Qt0TgVXleBUvnzOaVUrTs7Qm5x_EkI0Efw1OqPSMKW1OkfD1RbDfk7OQwhLcAl7l9q4XwPkGZLLgPsUJzwPgFuXx26M0-phBvwYYElxXjLObjd2JQ5rl2JYM2S8d9t5iLthDQE_C-W36FXvQoZ3p3iBftx-fmq-VvcPX-6aq_vKC2nmqjMtBe60aL2SoIXS0mnHTU2Mqlsqme-9ASZAmVJ2NWOUSq2c8aaXAhy_QB-PursUfy9ltp3GfDjObSEu2dblbslr9l-QEcEoV7qAn46gTzHnBL3dpXFyabWU2IMD9rqxBwdscaDQH06ySztB9489vbwA1REYy1_2f_su_Sq7cSXt9ydhpWjIt5vm1kr-B4FqkdM</recordid><startdate>20050501</startdate><enddate>20050501</enddate><creator>Zorn, Holger</creator><creator>Bouws, Henning</creator><creator>Takenberg, Meike</creator><creator>Nimtz, Manfred</creator><creator>Getzlaff, Rita</creator><creator>Breithaupt, Dietmar E.</creator><creator>Berger, Ralf G.</creator><general>Walter de Gruyter</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20050501</creationdate><title>An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters</title><author>Zorn, Holger ; 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Under native conditions, the enzyme exhibited a molecular mass of 430 kDa, and SDS-PAGE data suggested a composition of eight identical subunits. Biochemical characterisation of the purified protein showed an isoelectric point of 4.5, and ideal hydrolysis conditions were observed at pH 5.8 and 40°C. Partial amino acid sequences were derived from N-terminal Edman degradation and from mass spectrometric ab initio sequencing of internal peptides. An 1861-bp cDNA containing an open reading frame of 1641 bp was cloned from a cDNA library that showed ca. 40% homology to Candida rugosa lipases. The P. sapidus carboxylesterase represents the first enzyme of the lipase/esterase family from a basidiomycetous fungus that has been characterised at the molecular level.</abstract><cop>Germany</cop><pub>Walter de Gruyter</pub><pmid>15927887</pmid><doi>10.1515/BC.2005.052</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1431-6730 |
| ispartof | Biological chemistry, 2005-05, Vol.386 (5), p.435-440 |
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| language | eng |
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| source | MEDLINE; De Gruyter journals |
| subjects | Amino Acid Sequence Basidiomycetes Candida rugosa Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - isolation & purification carotenoids cDNA library Esters - chemistry Extracellular Fluid - enzymology fungi Hydrolysis Isoelectric Point lipase Lipase - chemistry Lipase - isolation & purification Models, Molecular Molecular Sequence Data Pleurotus Pleurotus - enzymology Protein Conformation Xanthophylls - chemistry |
| title | An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters |
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