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Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase fromCoprinopsis cinerea
- Source :
- Biotechnology and Bioengineering, Digital.CSIC. Repositorio Institucional del CSIC, instname
- Publication Year :
- 2013
-
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 w-1 and w-2 positions (only at the w-2 position in myristoleic acid). Alkyl esters of fatty acids and monoglycerides were also w-1 or w-2 hydroxylated, but di- and tri-glycerides were not modified. Fatty alcohols yielded hydroxy derivatives at the w-1 or w-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.<br />This study was funded by the PEROXICATS (KBBE-2010-4-265397) EU project. E.D. Babot thanks the Spanish CSIC for a JAE fellowship co-financed by FSE. R. Ullrich and M. Hofrichter are acknowledged for providing wild-type A. aegerita peroxygenase preparation.
- Subjects :
- Stereochemistry
Bioengineering
010402 general chemistry
Hydroxylation
01 natural sciences
Applied Microbiology and Biotechnology
Gas Chromatography-Mass Spectrometry
Mixed Function Oxygenases
03 medical and health sciences
chemistry.chemical_compound
Unspecific peroxygenase
Alkanes
Organic chemistry
Fatty acids
030304 developmental biology
Alkane
chemistry.chemical_classification
Fatty alcohols
0303 health sciences
biology
Agrocybe
Fatty Acids
Peroxygenase
biology.organism_classification
Recombinant Proteins
3. Good health
0104 chemical sciences
Coprinopsis cinerea
chemistry
Biocatalysis
Myristoleic acid
Heterologous expression
Fatty Alcohols
Agaricales
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 00063592
- Volume :
- 110
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- Biotechnology and Bioengineering
- Accession number :
- edsair.doi.dedup.....7feed1257994f3a54b36956f3b1c4cd5
- Full Text :
- https://doi.org/10.1002/bit.24904