Journal article

Publication year: 2009

Pages: 202-207

Journal: Journal of Molecular Catalysis B: Enzymatic

Volume number: 61

Issue number: 3-4

ISSN: 1381-1177

DOI Link: https://doi.org/10.1016/j.molcatb.2009.07.001

Publisher: Elsevier

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 by 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 similar to 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.

Harvard Citation style: Fraatz, M., Riemer, S., Stöber, R., Kaspera, R., Nimtz, M., Berger, R., et al. (2009) A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone, Journal of Molecular Catalysis B: Enzymatic, 61(3-4), pp. 202-207. https://doi.org/10.1016/j.molcatb.2009.07.001

APA Citation style: Fraatz, M., Riemer, S., Stöber, R., Kaspera, R., Nimtz, M., Berger, R., & Zorn, H. (2009). A novel oxygenase from Pleurotus sapidus transforms valencene to nootkatone. Journal of Molecular Catalysis B: Enzymatic. 61(3-4), 202-207. https://doi.org/10.1016/j.molcatb.2009.07.001