Recent developments in the use of peroxygenases – Exploring their high potential in selective oxyfunctionalisations

Hobisch, Markus; Holtmann, Dirk; Santos, Patricia Gómez de; Alcalde, Miguel; Hollmann, Frank; Kara, Selin

doi:10.1016/j.biotechadv.2020.107615

Cited by 146 publications

(147 citation statements)

References 118 publications

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“…Peroxygenases are receiving increased attention as selective oxyfunctionalization catalysts. 1 Compared to the well-known P450 monooxygenases, peroxygenases exhibit a significantly simpler molecular architecture and regeneration scheme. Both enzyme classes utilize an oxyferryl heme (compound I, Cpd I, Scheme 1 c) as oxygenation species.…”

Section: Introductionmentioning

confidence: 99%

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Tonin

Tieves

Willot

et al. 2021

Org. Process Res. Dev.

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The pilot-scale production of the peroxygenase from Agrocybe aegerita (r Aae UPO) is demonstrated. In a fed-batch fermentation of the recombinant Pichia pastoris, the enzyme was secreted into the culture medium to a final concentration of 0.29 g L –1 corresponding to 735 g of the peroxygenase in 2500 L of the fermentation broth after 6 days. Due to nonoptimized downstream processing, only 170 g of the enzyme has been isolated. The preparative usefulness of the so-obtained enzyme preparation has been demonstrated at a semipreparative scale (100 mL) as an example of the stereoselective hydroxylation of ethyl benzene. Using an adjusted H 2 O 2 feed rate, linear product formation was observed for 7 days, producing more than 5 g L –1 ( R )-1-phenyl ethanol. The biocatalyst performed more than 340.000 catalytic turnovers (942 g of the product per gram of r Aae UPO).

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Section: Introductionmentioning

confidence: 99%

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Tonin

Tieves

Willot

et al. 2021

Org. Process Res. Dev.

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“…Carbon nitrides are used to catalyse the formation of O 2 and H 2 via water oxidation [10] and the production of hydrogen peroxide from oxygen and alcohols, which requires the reduction of O 2 . [11] Hydrogen peroxide can then be used as stoichiometric oxidant in the enantioselective hydroxylation of ethylbenzene derivatives catalysed by the unspecific peroxygenase (UPO) [12] from A. aegerita [13] (AaeUPO) acting as chiral catalyst. [14] We hypothesized that a chromoselective activation of CN-OA-m with green light enables the selective formation of H 2 O 2 in the presence of ethylbenzene (1) and the AaeUPO, which in turn catalyses the asymmetric hydroxylation of 1 (Figure 2).…”

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confidence: 99%

Chromoselective Photocatalysis Enables Stereocomplementary Biocatalytic Pathways**

et al. 2021

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Controlling the selectivity of a chemical reaction with external stimuli is common in thermal processes, but rare in visible-light photocatalysis. Here we show that the redox potential of a carbon nitride photocatalyst (CN-OA-m) can be tuned by changing the irradiation wavelength to generate electron holes with different oxidation potentials. This tuning was the key to realizing photo-chemo-enzymatic cascades that give either the (S)-or the (R)-enantiomer of phenylethanol. In combination with an unspecific peroxygenase from Agrocybe aegerita, green light irradiation of CN-OA-m led to the enantioselective hydroxylation of ethylbenzene to (R)-1-phenylethanol (99 % ee). In contrast, blue light irradiation triggered the photocatalytic oxidation of ethylbenzene to acetophenone, which in turn was enantioselectively reduced with an alcohol dehydrogenase from Rhodococcus ruber to form (S)-1-phenylethanol (93 % ee).

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“…The catalytic glutamic acid residue in UPOs is well known to coordinate to histidine or arginine stabilising the negative charge formed at the acid-base catalyst. [1,17] MD simulations proved that H88 can establish persistent H-bond interactions with both E158 and E158D ( Fig. S11).…”

Section: Unspecificmentioning

confidence: 96%

Accessing Chemo- and Regioselective Benzylic and Aromatic Oxidations by Protein Engineering of an Unspecific Peroxygenase

Knorrscheidt¹,

Soler²,

Hünecke³

et al. 2020

Preprint

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Unspecific peroxygenases (UPOs) enable oxyfunctionalisations of a broad substrate range with unparalleled activities. Tailoring these enzymes for chemo- and regioselective transformations represents a grand challenge due to the difficulties in their heterologous productions. Herein, we performed a protein engineering in S. cerevisiae with the novel MthUPO. Experimental approaches were combined with computational modelling resulting in the screening of more than 5,300 transformants. This protein engineering led to a significant reshaping of the active site as elucidated by molecular dynamics. The kcat/Km was improved by 16.5-fold. Variants were identified with high chemo- and regioselectivities in the oxyfunctionalisation of aromatic and benzylic carbons, respectively. The benzylic hydroxylation was demonstrated to perform with excellent enantioselectivities of 95 % ee. Additionally, the first reported effective exchange of the conserved catalytic Glu residue was observed.

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Recent developments in the use of peroxygenases – Exploring their high potential in selective oxyfunctionalisations

Cited by 146 publications

References 118 publications

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Chromoselective Photocatalysis Enables Stereocomplementary Biocatalytic Pathways**

Accessing Chemo- and Regioselective Benzylic and Aromatic Oxidations by Protein Engineering of an Unspecific Peroxygenase

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