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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Walter de Gruyter ; 2005 |
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Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 386(2005), 5 vom: 05. Juli, Seite 435-440 |
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volume:386 ; year:2005 ; number:5 ; day:05 ; month:07 ; pages:435-440 ; extent:6 |
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10.1515/BC.2005.052 |
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10.1515/BC.2005.052 doi artikel_Grundlieferung.pp (DE-627)NLEJ246519266 DE-627 ger DE-627 rakwb An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters Walter de Gruyter 2005 6 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Walter de Gruyter Berlin New York 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. Walter de Gruyter Online Zeitschriften carotenoids cDNA library fungi lipase Zorn, Holger oth Bouws, Henning oth Takenberg, Meike oth Nimtz, Manfred oth Getzlaff, Rita oth Breithaupt, Dietmar E. oth Berger, Ralf G. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 386(2005), 5 vom: 05. Juli, Seite 435-440 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:386 year:2005 number:5 day:05 month:07 pages:435-440 extent:6 https://doi.org/10.1515/BC.2005.052 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 386 2005 5 05 07 435-440 6 |
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10.1515/BC.2005.052 doi artikel_Grundlieferung.pp (DE-627)NLEJ246519266 DE-627 ger DE-627 rakwb An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters Walter de Gruyter 2005 6 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Walter de Gruyter Berlin New York 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. Walter de Gruyter Online Zeitschriften carotenoids cDNA library fungi lipase Zorn, Holger oth Bouws, Henning oth Takenberg, Meike oth Nimtz, Manfred oth Getzlaff, Rita oth Breithaupt, Dietmar E. oth Berger, Ralf G. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 386(2005), 5 vom: 05. Juli, Seite 435-440 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:386 year:2005 number:5 day:05 month:07 pages:435-440 extent:6 https://doi.org/10.1515/BC.2005.052 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 386 2005 5 05 07 435-440 6 |
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10.1515/BC.2005.052 doi artikel_Grundlieferung.pp (DE-627)NLEJ246519266 DE-627 ger DE-627 rakwb An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters Walter de Gruyter 2005 6 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Walter de Gruyter Berlin New York 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. Walter de Gruyter Online Zeitschriften carotenoids cDNA library fungi lipase Zorn, Holger oth Bouws, Henning oth Takenberg, Meike oth Nimtz, Manfred oth Getzlaff, Rita oth Breithaupt, Dietmar E. oth Berger, Ralf G. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 386(2005), 5 vom: 05. Juli, Seite 435-440 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:386 year:2005 number:5 day:05 month:07 pages:435-440 extent:6 https://doi.org/10.1515/BC.2005.052 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 386 2005 5 05 07 435-440 6 |
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10.1515/BC.2005.052 doi artikel_Grundlieferung.pp (DE-627)NLEJ246519266 DE-627 ger DE-627 rakwb An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters Walter de Gruyter 2005 6 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Walter de Gruyter Berlin New York 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. Walter de Gruyter Online Zeitschriften carotenoids cDNA library fungi lipase Zorn, Holger oth Bouws, Henning oth Takenberg, Meike oth Nimtz, Manfred oth Getzlaff, Rita oth Breithaupt, Dietmar E. oth Berger, Ralf G. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 386(2005), 5 vom: 05. Juli, Seite 435-440 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:386 year:2005 number:5 day:05 month:07 pages:435-440 extent:6 https://doi.org/10.1515/BC.2005.052 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 386 2005 5 05 07 435-440 6 |
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10.1515/BC.2005.052 doi artikel_Grundlieferung.pp (DE-627)NLEJ246519266 DE-627 ger DE-627 rakwb An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters Walter de Gruyter 2005 6 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Walter de Gruyter Berlin New York 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. Walter de Gruyter Online Zeitschriften carotenoids cDNA library fungi lipase Zorn, Holger oth Bouws, Henning oth Takenberg, Meike oth Nimtz, Manfred oth Getzlaff, Rita oth Breithaupt, Dietmar E. oth Berger, Ralf G. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 386(2005), 5 vom: 05. Juli, Seite 435-440 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:386 year:2005 number:5 day:05 month:07 pages:435-440 extent:6 https://doi.org/10.1515/BC.2005.052 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 386 2005 5 05 07 435-440 6 |
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an extracellular carboxylesterase from the basidiomycete pleurotus sapidus hydrolyses xanthophyll esters |
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An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters |
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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. © Walter de Gruyter Berlin New York |
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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. © Walter de Gruyter Berlin New York |
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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. © Walter de Gruyter Berlin New York |
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10.1515/BC.2005.052 |
| up_date |
2024-07-06T08:42:09.023Z |
| _version_ |
1803818451887718400 |
| fullrecord_marcxml |
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7.4016743 |