Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Gonzalo, Gonzalo de; Alcántara, Andrés R.

doi:10.3390/catal11050605

Cited by 19 publications

(29 citation statements)

References 103 publications

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“…Due to the growing emphasis on sustainable large-scale production of chemicals and pharmaceuticals, enzymatic processes, particularly those associated with redox enzymes, have gained traction over the years as reflected in several recent Review articles. [37][38][39][40] For NAD(P)-coupled redox enzymes, cofac-tor regeneration is essential for practical implementation. Two modes of enzymatic regeneration are (i) substrate-coupled and (ii) enzyme-coupled reactions.…”

Section: Types Of Enzymatic Regeneration Methodsmentioning

confidence: 99%

Redox Biocatalysis: Quantitative Comparisons of Nicotinamide Cofactor Regeneration Methods

2022

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Enzymatic processes, particularly those capable of performing redox reactions, have recently been of growing research interest. Substrate specificity, optimal activity at mild temperatures, high selectivity, and yield are among the desirable characteristics of these oxidoreductase catalyzed reactions. Nicotinamide adenine dinucleotide (phosphate) or NAD(P)H‐dependent oxidoreductases have been extensively studied for their potential applications like biosynthesis of chiral organic compounds, construction of biosensors, and pollutant degradation. One of the main challenges associated with making these processes commercially viable is the regeneration of the expensive cofactors required by the enzymes. Numerous efforts have pursued enzymatic regeneration of NAD(P)H by coupling a substrate reduction with a complementary enzyme catalyzed oxidation of a co‐substrate. While offering excellent selectivity and high total turnover numbers, such processes involve complicated downstream product separation of a primary product from the coproducts and impurities. Alternative methods comprising chemical, electrochemical, and photochemical regeneration have been developed with the goal of enhanced efficiency and operational simplicity compared to enzymatic regeneration. Despite the goal, however, the literature rarely offers a meaningful comparison of the total turnover numbers for various regeneration methodologies. This comprehensive Review systematically discusses various methods of NAD(P)H cofactor regeneration and quantitatively compares performance across the numerous methods. Further, fundamental barriers to enhanced cofactor regeneration in the various methods are identified, and future opportunities are highlighted for improving the efficiency and sustainability of commercially viable oxidoreductase processes for practical implementation.

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Section: Types Of Enzymatic Regeneration Methodsmentioning

confidence: 99%

Redox Biocatalysis: Quantitative Comparisons of Nicotinamide Cofactor Regeneration Methods

2022

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“…In particular, cyclohexanone monooxygenase (CHMO) has been extensively investigated for the synthesis of ε-caprolactone, an important precursor for polymer synthesis (Schmidt et al, 2015;Scherkus et al, 2016;Engel et al, 2019a). Generally, most cascades have been developed by coupling various alcohol dehydrogenases (ADHs) (Bornadel et al, 2015;Schmidt et al, 2015;Scherkus et al, 2016;Scherkus et al, 2017;Engel et al, 2019b;de Gonzalo and Alcántara, 2021) as well as newly reported thioredoxin/thioredoxin reductases pairs (Zhang et al, 2022) with CHMO to form redox-neutral self-sufficient systems. Despite these advances, in most one-pot systems, substrate concentrations have been used up to 100 mM given the strong substrate and product inhibition.…”

Section: Introductionmentioning

confidence: 99%

Design of fusion enzymes for biocatalytic applications in aqueous and non-aqueous media

Ying-jie

Zhang

Vernet

et al. 2022

Front. Bioeng. Biotechnol.

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Biocatalytic cascades play a fundamental role in sustainable chemical synthesis. Fusion enzymes are one of the powerful toolboxes to enable the tailored combination of multiple enzymes for efficient cooperative cascades. Especially, this approach offers a substantial potential for the practical application of cofactor-dependent oxidoreductases by forming cofactor self-sufficient cascades. Adequate cofactor recycling while keeping the oxidized/reduced cofactor in a confined microenvironment benefits from the fusion fashion and makes the use of oxidoreductases in harsh non-aqueous media practical. In this mini-review, we have summarized the application of various fusion enzymes in aqueous and non-aqueous media with a focus on the discussion of linker design within oxidoreductases. The design and properties of the reported linkers have been reviewed in detail. Besides, the substrate loadings in these studies have been listed to showcase one of the key limitations (low solubility of hydrophobic substrates) of aqueous biocatalysis when it comes to efficiency and economic feasibility. Therefore, a straightforward strategy of applying non-aqueous media has been briefly discussed while the potential of using the fusion oxidoreductase of interest in organic media was highlighted.

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“…Ketone 1c is oxidized to 2b and to 4-oxahomoadamantane-5-one (lactone 2c) (Bayer-Williger reaction) [22,23].…”

Section: Introductionmentioning

confidence: 99%

One-Stage Catalytic Oxidation of Adamantane to Tri-, Tetra-, and Penta-Ols

et al. 2021

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Tertiary tetraols of adamantane (C10H16, Tricyclo[3.3.1.1(3,7)]decan) have been widely used for the synthesis of highly symmetric compounds with unique physical and chemical properties. The methods for one-stage simultaneously selective, deep, and cheap oxidation of adamantane to tetraols of different structures have not yet been developed. In this research, chemically simple, cheap, and environmentally friendly reagents are used and that is the first step in this direction. The conditions, under which the impact of a hydrogen peroxide water solution on adamantane dissolved in acetonitrile results in full conversion of adamantane and formation of a total 72% mixture of its tri-, tetra-, and penta-oxygenated products, predominantly poliols, have been found. Conversion and adamantane oxidation depth are shown to depend on the ratio of components of the water-acetonitrile solution and the method of oxidizer solution introduction when using the dimer form of 1:1 dimethylglyoxime and copper dichloride complex as a catalyst. Under the conditions of mass-spectrometry ionization by electrons (70 eV), fragmentation across three C–C bonds of the molecular ions framework of adamantane tertiary alcohols Ad(OH)n in the range n = 0–4 increases linearly with the rise of n.

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Multienzymatic Processes Involving Baeyer–Villiger Monooxygenases

Cited by 19 publications

References 103 publications

Redox Biocatalysis: Quantitative Comparisons of Nicotinamide Cofactor Regeneration Methods

Redox Biocatalysis: Quantitative Comparisons of Nicotinamide Cofactor Regeneration Methods

Design of fusion enzymes for biocatalytic applications in aqueous and non-aqueous media

One-Stage Catalytic Oxidation of Adamantane to Tri-, Tetra-, and Penta-Ols

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