FOx News: Towards Methanol‐driven Biocatalytic Oxyfunctionalisation Reactions

Willot, Sébastien J.‐P.; Hoang, Manh Dat; Paul, Caroline E.; Alcalde, Miguel; Arends, Isabel W. C. E.; Bommarius, Andreas S.; Bommarius, Bettina; Hollmann, Frank

doi:10.1002/cctc.202000197

Cited by 16 publications

(10 citation statements)

References 34 publications

(8 reference statements)

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“…200 mL after 7 days). Further developments therefore will focus on the application of in situ H 2 O 2 generation from O 2 using simple reductants such as formate − or methanol. − …”

Section: Discussionmentioning

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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“…200 mL after 7 days). Further developments therefore will focus on the application of in situ H 2 O 2 generation from O 2 using simple reductants such as formate − or methanol. − …”

Section: Discussionmentioning

confidence: 99%

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Tonin

Tieves

Willot

et al. 2021

Org. Process Res. Dev.

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“…Supplying the reaction over time with H 2 O 2 instead of adding it stoichiometrically has proved to be a beneficial strategy to achieve maximal product formation. Several smart procedures to maintain low H 2 O 2 concentrations by continuous in situ H 2 O 2 generation systems have been developed, for example, the utilization of biocatalysts such as formate oxidase (Fox) were employed. − Further concepts are based on the usage of light-driven reactions, gold–palladium nanoparticles, or radiolytic water splitting to produce H 2 O 2 . − …”

Section: Iron-dependent Enzymesmentioning

confidence: 99%

Enzymatic Hydroxylations of sp³-Carbons

et al. 2021

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Enzymatic hydroxylation of activated and nonactivated sp 3 -carbons attracts keen interest from the chemistry community as it is one of the most challenging tasks in organic synthesis. Nature provides a vast number of enzymes with an enormous catalytic versatility to fulfill this task. Given that those very different enzymes have a distinct specificity in substrate scope, selectivity, activity, stability, and catalytic cycle, it is interesting to outline similarities and differences. In this Review, we intend to delineate which enzymes possess considerable advantages within specific issues. Heterologous production, crystal structure availability, enzyme engineering potential, and substrate promiscuity are essential factors for the applicability of these biocatalysts.

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“…Photochemical approaches for the in situ reduction of O 2 to H 2 O 2 are attractive because they also enable using sacrificial electron donors such as EDTA , or simple alcohols . Enzymatic H 2 O 2 generation methods are more restricted in terms of sacrificial electron donors that can be used. − Furthermore, combining photocatalysis with biocatalysis offers new possibilities for organic synthesis ranging from new regeneration approaches for cofactor-dependent enzymes, − photoenzymatic cascades, and “new to nature” reactions catalyzed by photoexcited enzymes. − Yet, the combination of photocatalysis with biocatalysis is not always unproblematic due to issues of photobleaching and formation of reactive oxygen species. − …”

Section: Introductionmentioning

confidence: 99%

Water-Soluble Anthraquinone Photocatalysts Enable Methanol-Driven Enzymatic Halogenation and Hydroxylation Reactions

et al. 2020

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Peroxyzymes simply use H 2 O 2 as a cosubstrate to oxidize a broad range of inert C–H bonds. The lability of many peroxyzymes against H 2 O 2 can be addressed by a controlled supply of H 2 O 2 , ideally in situ. Here, we report a simple, robust, and water-soluble anthraquinone sulfonate (SAS) as a promising organophotocatalyst to drive both haloperoxidase-catalyzed halogenation and peroxygenase-catalyzed oxyfunctionalization reactions. Simple alcohols, methanol in particular, can be used both as a cosolvent and an electron donor for H 2 O 2 generation. Very promising turnover numbers for the biocatalysts of up to 318 000 have been achieved.

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FOx News: Towards Methanol‐driven Biocatalytic Oxyfunctionalisation Reactions

Cited by 16 publications

References 34 publications

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Enzymatic Hydroxylations of sp³-Carbons

Water-Soluble Anthraquinone Photocatalysts Enable Methanol-Driven Enzymatic Halogenation and Hydroxylation Reactions

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FOx News: Towards Methanol‐driven Biocatalytic Oxyfunctionalisation Reactions

Cited by 16 publications

References 34 publications

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Pilot-Scale Production of Peroxygenase from Agrocybe aegerita

Enzymatic Hydroxylations of sp3-Carbons

Water-Soluble Anthraquinone Photocatalysts Enable Methanol-Driven Enzymatic Halogenation and Hydroxylation Reactions

Contact Info

Product

Resources

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Enzymatic Hydroxylations of sp³-Carbons