Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea
- 20 March 2013
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 110 (9), 2323-2332
- https://doi.org/10.1002/bit.24904
Abstract
The goal of this study is the selective oxyfunctionalization of aliphatic compounds under mild and environmentally friendly conditions using a low-cost enzymatic biocatalyst. This could be possible taking advantage from a new peroxidase type that catalyzes monooxygenase reactions with H2O2 as the only cosubstrate (peroxygenase). With this purpose, recombinant peroxygenase, from gene mining in the sequenced genome of Coprinopsis cinerea and heterologous expression using an industrial fungal host, is tested for the first time on aliphatic substrates. The reaction on free and esterified fatty acids and alcohols, and long-chain alkanes was followed by gas chromatography, and the different reaction products were identified by mass spectrometry. Regioselective hydroxylation of saturated/unsaturated fatty acids was observed at the ω-1 and ω-2 positions (only at the ω-2 position in myristoleic acid). Alkyl esters of fatty acids and monoglycerides were also ω-1 or ω-2 hydroxylated, but di- and tri-glycerides were not modified. Fatty alcohols yielded hydroxy derivatives at the ω-1 or ω-2 positions (diols) but also fatty acids and their hydroxy derivatives. Interestingly, the peroxygenase was able to oxyfunctionalize alkanes giving, in addition to alcohols at positions 2 or 3, dihydroxylated derivatives at both sides of the molecule. The predominance of mono- or di-hydroxylated derivatives seems related to the higher or lower proportion of acetone, respectively, in the reaction medium. The recombinant C. cinerea peroxygenase appears as a promising biocatalyst for alkane activation and production of aliphatic oxygenated derivatives, with better properties than the previously reported peroxygenase from Agrocybe aegerita, and advantages related to its recombinant nature for enzyme engineering and industrial production. Biotechnol. Bioeng. 2013; 110:2323–2332.Keywords
This publication has 30 references indexed in Scilit:
- Selective hydroxylation of alkanes by an extracellular fungal peroxygenaseThe FEBS Journal, 2011
- Structural control of cytochrome P450-catalyzed ω-hydroxylationArchives of Biochemistry and Biophysics, 2011
- High-yield production of aromatic peroxygenase by the agaric fungus Marasmius rotulaAMB Express, 2011
- Crystallization of a 45 kDa peroxygenase/peroxidase from the mushroomAgrocybe aegeritaand structure determination by SAD utilizing only the haem ironActa Crystallographica Section F Structural Biology and Crystallization Communications, 2010
- The Coprophilous Mushroom Coprinus radians Secretes a Haloperoxidase That Catalyzes Aromatic PeroxygenationApplied and Environmental Microbiology, 2007
- Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and AldehydesApplied and Environmental Microbiology, 2004
- Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylaseNature Biotechnology, 2002
- Roles of key active-site residues in flavocytochrome P450 BM3Biochemical Journal, 1999
- The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3Journal of Biological Chemistry, 1996
- ω-1, ω-2 and ω-3 Hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megatyeriumBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1975