A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity
Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was sem...
Ausführliche Beschreibung
Autor*in: |
Nina-Katharina Krahe [verfasserIn] Ralf G. Berger [verfasserIn] Franziska Ersoy [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Schlagwörter: |
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Übergeordnetes Werk: |
In: Molecules - MDPI AG, 2003, 25(2020), 7, p 1536 |
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Übergeordnetes Werk: |
volume:25 ; year:2020 ; number:7, p 1536 |
Links: |
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DOI / URN: |
10.3390/molecules25071536 |
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Katalog-ID: |
DOAJ06433077X |
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520 | |a Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. | ||
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10.3390/molecules25071536 doi (DE-627)DOAJ06433077X (DE-599)DOAJ6cdd7ce6bcea484ca3e9252a51fe1838 DE-627 ger DE-627 rakwb eng QD241-441 Nina-Katharina Krahe verfasserin aut A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. alkene cleavage aryl alkenes basidiomycota biocatalysis carotene degradation dye-decolorizing peroxidase (DyP) Organic chemistry Ralf G. Berger verfasserin aut Franziska Ersoy verfasserin aut In Molecules MDPI AG, 2003 25(2020), 7, p 1536 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:7, p 1536 https://doi.org/10.3390/molecules25071536 kostenfrei https://doaj.org/article/6cdd7ce6bcea484ca3e9252a51fe1838 kostenfrei https://www.mdpi.com/1420-3049/25/7/1536 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 7, p 1536 |
spelling |
10.3390/molecules25071536 doi (DE-627)DOAJ06433077X (DE-599)DOAJ6cdd7ce6bcea484ca3e9252a51fe1838 DE-627 ger DE-627 rakwb eng QD241-441 Nina-Katharina Krahe verfasserin aut A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. alkene cleavage aryl alkenes basidiomycota biocatalysis carotene degradation dye-decolorizing peroxidase (DyP) Organic chemistry Ralf G. Berger verfasserin aut Franziska Ersoy verfasserin aut In Molecules MDPI AG, 2003 25(2020), 7, p 1536 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:7, p 1536 https://doi.org/10.3390/molecules25071536 kostenfrei https://doaj.org/article/6cdd7ce6bcea484ca3e9252a51fe1838 kostenfrei https://www.mdpi.com/1420-3049/25/7/1536 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 7, p 1536 |
allfields_unstemmed |
10.3390/molecules25071536 doi (DE-627)DOAJ06433077X (DE-599)DOAJ6cdd7ce6bcea484ca3e9252a51fe1838 DE-627 ger DE-627 rakwb eng QD241-441 Nina-Katharina Krahe verfasserin aut A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. alkene cleavage aryl alkenes basidiomycota biocatalysis carotene degradation dye-decolorizing peroxidase (DyP) Organic chemistry Ralf G. Berger verfasserin aut Franziska Ersoy verfasserin aut In Molecules MDPI AG, 2003 25(2020), 7, p 1536 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:7, p 1536 https://doi.org/10.3390/molecules25071536 kostenfrei https://doaj.org/article/6cdd7ce6bcea484ca3e9252a51fe1838 kostenfrei https://www.mdpi.com/1420-3049/25/7/1536 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 7, p 1536 |
allfieldsGer |
10.3390/molecules25071536 doi (DE-627)DOAJ06433077X (DE-599)DOAJ6cdd7ce6bcea484ca3e9252a51fe1838 DE-627 ger DE-627 rakwb eng QD241-441 Nina-Katharina Krahe verfasserin aut A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. alkene cleavage aryl alkenes basidiomycota biocatalysis carotene degradation dye-decolorizing peroxidase (DyP) Organic chemistry Ralf G. Berger verfasserin aut Franziska Ersoy verfasserin aut In Molecules MDPI AG, 2003 25(2020), 7, p 1536 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:25 year:2020 number:7, p 1536 https://doi.org/10.3390/molecules25071536 kostenfrei https://doaj.org/article/6cdd7ce6bcea484ca3e9252a51fe1838 kostenfrei https://www.mdpi.com/1420-3049/25/7/1536 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2020 7, p 1536 |
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A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity |
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Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. |
abstractGer |
Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. |
abstract_unstemmed |
Alkene cleavage is a possibility to generate aldehydes with olfactory properties for the fragrance and flavor industry. A dye-decolorizing peroxidase (DyP) of the basidiomycete <i<Pleurotus sapidus</i< (PsaPOX) cleaved the aryl alkene <i<trans</i<-anethole. The PsaPOX was semi-purified from the mycelium via FPLC, and the corresponding gene was identified. The amino acid sequence as well as the predicted tertiary structure showed typical characteristics of DyPs as well as a non-canonical Mn<sup<2+</sup<-oxidation site on its surface. The gene was expressed in <i<Komagataella pfaffii</i< GS115 yielding activities up to 142 U/L using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) as substrate. PsaPOX exhibited optima at pH 3.5 and 40 °C and showed highest peroxidase activity in the presence of 100 µM H<sub<2</sub<O<sub<2</sub< and 25 mM Mn<sup<2+</sup<. PsaPOX lacked the typical activity of DyPs towards anthraquinone dyes, but oxidized Mn<sup<2+</sup< to Mn<sup<3+</sup<. In addition, bleaching of <i<β</i<-carotene and annatto was observed. Biotransformation experiments verified the alkene cleavage activity towards the aryl alkenes (<i<E</i<)-methyl isoeugenol, <i<α</i<-methylstyrene, and <i<trans</i<-anethole, which was increased almost twofold in the presence of Mn<sup<2+</sup<. The resultant aldehydes are olfactants used in the fragrance and flavor industry. PsaPOX is the first described DyP with alkene cleavage activity towards aryl alkenes and showed potential as biocatalyst for flavor production. |
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7, p 1536 |
title_short |
A DyP-Type Peroxidase of <i<Pleurotus sapidus</i< with Alkene Cleaving Activity |
url |
https://doi.org/10.3390/molecules25071536 https://doaj.org/article/6cdd7ce6bcea484ca3e9252a51fe1838 https://www.mdpi.com/1420-3049/25/7/1536 https://doaj.org/toc/1420-3049 |
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Ralf G. Berger Franziska Ersoy |
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