We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Cell-free one-pot conversion of (+)-valencene to (+)-nootkatone by a unique dye-decolorizing peroxidase combined with a laccase from <italic>Funalia trogii</italic>.
- Authors
Kolwek, Julia; Behrens, Christoph; Linke, Diana; Krings, Ulrich; Berger, Ralf G.
- Abstract
A combined system of a unique dye-decolorizing peroxidase (Ftr-DyP) and a laccase obtained from the basidiomycete <italic>Funalia trogii</italic> converted the precursor (+)-valencene completely to the high-value grapefruit flavour constituent (+)-nootkatone, reaching a concentration maximum of 1100 mg/L. In the presence of 1 mM Mn2+ and 2.5 mM <italic>p</italic>-coumaric acid, (+)-nootkatone was the predominating volatile product, and only traces of substrate and the nootkatols were detectable after 24 h. Hence, the two-enzyme-system reproduced the oxidizing activity observed before for the crude culture supernatant. The newly discovered Ftr-DyP was purified, sequenced and further characterized as a thermostable, non-glycosylated protein with a pH-optimum in the acidic range and a calculated mass of 52.3 kDa. Besides the typical activity of DyPs towards anthraquinone dyes, Ftr-DyP also oxidized Mn2+ and showed activity in the absence of hydrogen peroxide. Neither the DyP from <italic>Mycetinis scorodonius</italic> nor the manganese peroxidase from <italic>Nematoloma frowardii</italic> were able to replace Ftr-DyP in this reaction. A hypothetical reaction mechanism is presented.
- Subjects
BASIDIOMYCETES; NOOTKATONE; MANGANESE peroxidase; LACCASE; ANTHRAQUINONE dyes
- Publication
Journal of Industrial Microbiology & Biotechnology, 2018, Vol 45, Issue 2, p89
- ISSN
1367-5435
- Publication type
Article
- DOI
10.1007/s10295-017-1998-9