Synthesis of methyl propanoate by Baeyer–Villiger monooxygenases

Beek, Hugo L. van; Winter, Remko T.; Eastham, Graham R.; Fraaije, Marco W.

doi:10.1039/c4cc06489e

Cited by 22 publications

(27 citation statements)

References 24 publications

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“…They were able to produce the desired compounds in gram scale at ambient temperature, in water, in the presence of aerial oxygen instead of propellant-grade H 2 O 2 which is required for the chemical reaction. Another quite appealing approach was published by the group of Fraaije (van Beek et al 2014). They managed to find several BVMOs for the production of ethyl acetate (36) or methyl propionate (37) starting from 2-butanone (34).…”

Section: Potential Bvmo-mediated Industrial Processesmentioning

confidence: 99%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

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Baeyer-Villiger monooxygenases (BVMOs) are a very well-known and intensively studied class of flavin-dependent enzymes. Their substrate promiscuity, high chemo-, regio-, and enantioselectivity are prerequisites for the use in synthetic chemistry and should pave the way for successful industrial processes. Nonetheless, only a very limited number of industrial relevant transformations are known, mainly due to the lack of BVMOs stability and cofactor dependency. In this review, we focus on novel BVMO-mediated transformations, BVMOs in cascade type reactions, potential industrial applications, and how limitations have been tackled by the community. Special attention will be put on whole-cell immobilization strategies. We emphasize to bridge recent developments in fundamental research to industrial applications.

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Section: Potential Bvmo-mediated Industrial Processesmentioning

confidence: 99%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

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“…It is so far the only known industrial process from this class of enzymes, but conceptuala pplications tudies abound in the literature, [10] for example,s ynthesis of API intermediates, [11] metabolites, [12] aroma compounds, [13] polyester monomers, [14] or platform chemicals. [15] Despite the lack of knowledge about the originso f the poors tability,m ost other studies on stabilization chose to alter the protein structure-randomly, [21] or by design. [19,20] Their impact on the applicability of class BF MOs hasb een low,b ecause absolute quantitative data of improvement are inconclusive: (i)o perational (kinetic) stability,i fa ta ll determined, was so faro nly improvedw ithin an order of magnitude; [19][20][21] (ii)t he effecto fu nspecific additives provided only a1 .3-fold increase of the half-life (t 1/2 ); [17] (iii) the stabilizing effect of NADPH, described in as ingle instance on 4-hydroxyacetophenone monooxygenase, [22] wasn ever quantified;( iv) published values of CHMOst 1/2 span approx.t hree orders of magnitude (wild-type only,F igure 1).…”

Section: Introductionmentioning

confidence: 99%

Mutagenesis‐Independent Stabilization of Class B Flavin Monooxygenases in Operation

et al. 2017

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This paper describest he stabilizationo f flavin-dependent monooxygenases under reaction conditions,u sing an engineered formulation of additives (the natural cofactors NADPH andF AD,a nd superoxide dismutase and catalase as catalytic antioxidants). This way,a10 3 -t o1 0 4 -foldi ncrease of the half-life was reached without resource-intensive directed evolution or structure-dependent protein engineering methods. Thes tabilized enzymes are highly valuedf or theirs ynthetic potential in biotechnology and medicinalc hemistry (enantioselective sulfur, nitrogen and Baeyer-Villiger oxidations;o xidative human metabolism), but widespread application was so far hindered by their notoriousf ragility. Our technology immediately enables their use,d oes not require structural knowledge of the biocatalyst, and creates as trong basis for the targeted development of improvedvariants by mutagenesis.

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“…The development of a bio-based production process would mitigate these effects and exploit the potential of these methyl esters. Recent findings show that methyl propionate can be formed by enzymatic oxidation of 2-butanone (van Beek et al 2014 ). The fermentative production of 2-butanone has also been proposed, both in Escherichia coli (Yoneda et al 2014 ) and Saccharomyces cerevisiae (Ghiaci et al 2014 ).…”

Section: Introductionmentioning

confidence: 99%

Growth inhibition of S. cerevisiae, B. subtilis, and E. coli by lignocellulosic and fermentation products

Pereira

Verheijen

Straathof

2016

Appl Microbiol Biotechnol

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This paper describes the effect of several inhibiting components on three potential hosts for the bio-based production of methyl propionate, namely, wild-type Escherichia coli and Bacillus subtilis, and evolved Saccharomyces cerevisiae IMS0351. The inhibition by the lignocellulose-derived products 5-hydroxymethyl-2-furaldehyde, vanillin, and syringaldehyde and the fermentation products 2-butanol, 2-butanone, methyl propionate, and ethyl acetate has been assessed for these strains in defined medium. Multiple screenings were performed using small-scale cultures in both shake flasks and microtiter plates. Technical drawbacks revealed the limited applicability of the latter in this study. The microbial growth was characterized by means of a lag-time model, and the inhibitory thresholds were determined using product-inhibition models. The lignocellulose-derived products were found to be highly inhibitory, and none of the strains could grow in the presence of 2.0 g L−1 of product. From the fermentation products tested, methyl propionate had the most severe impact resulting in complete inhibition of all the strains when exposed to concentrations in the range of 12–18 g L−1. In general, S. cerevisiae and B. subtilis were comparatively more tolerant than E. coli to all the fermentation products, despite E. coli’s lower sensitivity towards vanillin. The results suggest that, overall, the strains investigated have good potential to be engineered and further established as hosts for the bio-based production of methyl esters.

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Synthesis of methyl propanoate by Baeyer–Villiger monooxygenases

Cited by 22 publications

References 24 publications

Baeyer-Villiger oxidations: biotechnological approach

Baeyer-Villiger oxidations: biotechnological approach

Mutagenesis‐Independent Stabilization of Class B Flavin Monooxygenases in Operation

Growth inhibition of S. cerevisiae, B. subtilis, and E. coli by lignocellulosic and fermentation products

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