Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 202-207 |
| Seitenumfang | 6 |
| Fachzeitschrift | Journal of Molecular Catalysis B: Enzymatic |
| Jahrgang | 61 |
| Ausgabenummer | 3-4 |
| Publikationsstatus | Veröffentlicht - 9 Juli 2009 |
Abstract
A selective and highly efficient allylic oxidation of the sesquiterpene (+)-valencene to (+)-nootkatone was achieved with lyophilisate of the basidiomycete Pleurotus sapidus. The responsible enzymatic activity was biochemically characterised and purified by chromatographic and electrophoretic methods. Peptide sequences obtained by mass spectrometry showed homologies to oxygenases from various ascomycetes. Based on the peptide sequences, the encoding cDNA was amplified from a cDNA library of P. sapidus by PCR. The cloned sequence consisted of 1309 bp with an open reading frame of 1191 bp. Based on database research, the translated amino acid sequence of 396 amino acids showed on the protein level homologies of ∼50% to putative lipoxygenases from Aspergillus fumigatus and Laccaria bicolor as well as 26% homology to the sequence of lipoxygenase-1 from soy bean (Glycine max). A lipoxygenase from a basidiomycetous fungus has not yet been characterised on a molecular level.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Katalyse
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Chemische Verfahrenstechnik (insg.)
- Prozesschemie und -technologie
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in: Journal of Molecular Catalysis B: Enzymatic, Jahrgang 61, Nr. 3-4, 09.07.2009, S. 202-207.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone
AU - Fraatz, Marco A.
AU - Riemer, Stephanie J.L.
AU - Stöber, Regina
AU - Kaspera, Rüdiger
AU - Nimtz, Manfred
AU - Berger, Ralf G.
AU - Zorn, Holger
PY - 2009/7/9
Y1 - 2009/7/9
N2 - A selective and highly efficient allylic oxidation of the sesquiterpene (+)-valencene to (+)-nootkatone was achieved with lyophilisate of the basidiomycete Pleurotus sapidus. The responsible enzymatic activity was biochemically characterised and purified by chromatographic and electrophoretic methods. Peptide sequences obtained by mass spectrometry showed homologies to oxygenases from various ascomycetes. Based on the peptide sequences, the encoding cDNA was amplified from a cDNA library of P. sapidus by PCR. The cloned sequence consisted of 1309 bp with an open reading frame of 1191 bp. Based on database research, the translated amino acid sequence of 396 amino acids showed on the protein level homologies of ∼50% to putative lipoxygenases from Aspergillus fumigatus and Laccaria bicolor as well as 26% homology to the sequence of lipoxygenase-1 from soy bean (Glycine max). A lipoxygenase from a basidiomycetous fungus has not yet been characterised on a molecular level.
AB - A selective and highly efficient allylic oxidation of the sesquiterpene (+)-valencene to (+)-nootkatone was achieved with lyophilisate of the basidiomycete Pleurotus sapidus. The responsible enzymatic activity was biochemically characterised and purified by chromatographic and electrophoretic methods. Peptide sequences obtained by mass spectrometry showed homologies to oxygenases from various ascomycetes. Based on the peptide sequences, the encoding cDNA was amplified from a cDNA library of P. sapidus by PCR. The cloned sequence consisted of 1309 bp with an open reading frame of 1191 bp. Based on database research, the translated amino acid sequence of 396 amino acids showed on the protein level homologies of ∼50% to putative lipoxygenases from Aspergillus fumigatus and Laccaria bicolor as well as 26% homology to the sequence of lipoxygenase-1 from soy bean (Glycine max). A lipoxygenase from a basidiomycetous fungus has not yet been characterised on a molecular level.
KW - Basidiomycete
KW - Biotransformation
KW - Nootkatone
KW - Oxygenase
KW - Valencene
UR - http://www.scopus.com/inward/record.url?scp=70349424066&partnerID=8YFLogxK
U2 - 10.1016/j.molcatb.2009.07.001
DO - 10.1016/j.molcatb.2009.07.001
M3 - Article
AN - SCOPUS:70349424066
VL - 61
SP - 202
EP - 207
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
SN - 1381-1177
IS - 3-4
ER -