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23 results on '"Hilberath, Thomas"'

2. Selective Peroxygenase‐Catalysed Oxidation of Phenols to Hydroquinones.

Author

Brasselet, Hugo, Schmitz, Fabian, Koschorreck, Katja, Urlacher, Vlada B., Hollmann, Frank, and Hilberath, Thomas

Subjects
PHENOLS, BIOCATALYSIS, PHENOL, ENZYMES, HYDROXYLATION
Abstract

An enzymatic method for the selective hydroxylation of phenols using a peroxygenase from Aspergillus brasiliensis (AbrUPO) is reported. A broad range of phenolic starting materials can be selectively transformed into the corresponding hydroquinones. Semi‐preparative syntheses of several hydroquinones were realised without further optimization pointing out the applicability of this enzyme as biocatalyst. [ABSTRACT FROM AUTHOR]

Published
2024
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4. Synthesis of Enantiopure Vicinal Halohydrins Using a Sequence of Haloperoxidase and Lipase.

Author

De Marchi, Elisa, Hilberath, Thomas, Zippilli, Claudio, Wever, Ron, Saladino, Raffaele, Hollmann, Frank, and Botta, Lorenzo

Subjects
*LIPASES, *KINETIC resolution, *ENANTIOMERIC purity, *ALKENES, *HALOGENATION
Abstract

Vicinal halohydrins are key building blocks to produce bioactive molecules and drugs, especially if they can be obtained in enantiomerically pure form. In this study, we present a bi‐enzymatic sequence that allows to obtain vic‐halohydrins through a photochemoenzymatic olefin hydroxy halogenation followed by a lipase catalysed kinetic resolution. The absolute configuration of the resulting products was determined using Mosher's method [ABSTRACT FROM AUTHOR]

Published
2024
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11. Toward Kilogram-Scale Peroxygenase-Catalyzed Oxyfunctionalization of Cyclohexane

Author

Hilberath, Thomas, van Oosten, Remco, Victoria, Juliet, Brasselet, Hugo, Alcalde, Miguel, Woodley, John M., Hollmann, Frank, Hilberath, Thomas, van Oosten, Remco, Victoria, Juliet, Brasselet, Hugo, Alcalde, Miguel, Woodley, John M., and Hollmann, Frank

Abstract

Mol-scale oxyfunctionalization of cyclohexane to cyclohexanol/cyclohexanone (KA-oil) using an unspecific peroxygenase is reported. Using AaeUPO from Agrocybe aegerita and simple H2O2 as an oxidant, cyclohexanol concentrations of more than 300 mM (>60% yield) at attractive productivities (157 mM h–1, approx. 15 g L–1 h–1) were achieved. Current limitations of the proposed biooxidation system have been identified paving the way for future improvements and implementation.

Published
2023

19. Additional file 1 of Evaluation of P450 monooxygenase activity in lyophilized recombinant E. coli cells compared to resting cells

Author

Hilberath, Thomas, Raffaele, Alessandra, Windeln, Leonie M., and Urlacher, Vlada B.

Abstract

Additional file 1: Table S1: Synthetic oligonucleotides for cloning. Table S2: Plasmids used in this study. Table S3: Analysis of testosterone 1 and metabolites 2-10 that were formed during CYP105D-mediated oxidation. Figure S1: Effect of freezing and glycerol addition during lyophilization on conversion catalyzed by E. coli C43 (DE3) pET22b-cyp105D + pCOLADuet- pdx-pdr-adh. E. coli cells were once or twice frozen at ��� 80��C and then lyophilized for either 24 h (black) or 48 h (grey). Figure S2: Exemplary LC/MS-chromatogram showing the oxidation of testosterone 1 to the products 2-10 by the CYP105D-based E. coli whole-cell biocatalyst (pink) in comparison to a negative control (black). Figure S3: SDS-PAGE analysis of E. coli C43 (DE3) strains for whole-cell biocatalysis. Figure S4: Effect of NADH addition on testosterone 1 conversion mediated by the lyophilized whole-cell catalyst without ADH. NADH was added up to four times (number in brackets) every 2 h.

Published
2021
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22. Draft Genome Sequences of Three Actinobacteria Strains Presenting New Candidate Organisms with High Potentials for Specific P450 Cytochromes

Author

Grumaz, Christian, primary, Vainshtein, Yevhen, additional, Kirstahler, Philipp, additional, Luetz, Stephan, additional, Kittelmann, Matthias, additional, Schroer, Kirsten, additional, Eggimann, Fabian K., additional, Czaja, Rico, additional, Vogel, Andreas, additional, Hilberath, Thomas, additional, Worsch, Anne, additional, Girhard, Marco, additional, Urlacher, Vlada B., additional, Sandberg, Marcel, additional, and Sohn, Kai, additional

Published
2017
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23. Ene‐Reductase‐Catalyzed Oxidation Reactions.

Author

Hengst, Jacob M.A., Wolder, Allison E., Sánchez, Marisa, Huijbers, Mieke M. E., Opperman, Diederik J., Gilles, Pierre, Martin, Juliette, Hilberath, Thomas, Hollmann, Frank, and Paul, Caroline E.

Subjects
*CONJUGATED systems, *CARBONYL compounds, *KINETIC resolution, *BIOCHEMICAL substrates, *ENZYMES
Abstract

Ene‐reductases from the old yellow enzyme (OYE) family have been traditionally employed in the reduction of conjugated C═C double bonds. This study explores the underutilized oxidative potential of OYEs, demonstrating their capability to catalyze the enantioselective desaturation of carbonyl compounds. Utilizing a deprotonated tyrosine residue as a catalytic base, we developed a method to enable OYE‐catalyzed desaturation at ambient temperature and alkaline pH without the need for high‐temperature conditions. Through screening of various OYE enzymes, we identified several candidates from different genera with enhanced desaturase activity across different substrates. This work broadens the scope of biocatalytic applications for OYEs, introducing a novel approach to the synthesis of chiral α,β‐unsaturated carbonyl compounds. [ABSTRACT FROM AUTHOR]

Published
2024
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