Recent developments in oxidative biocatalytic cascades

See, Willy Wei Li; Choo, Joel P.S.; Jung, Do-Yun; Li, Zhi

doi:10.1016/j.cogsc.2022.100700

Cited by 8 publications

(6 citation statements)

References 51 publications

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“…HXN-200 (SpEH) into five differently designed enzyme cascades shown in Figure 3 and listed in Table 4 . In this review article [ 163 ], other recent studies on new cascades using a tandem of EHs with styrene monooxygenases (SMO) connected with other enzymes to form cascades were presented. This confirmed the multifunctionality of EHs for the production of important building blocks and other chemical specialties using enzyme cascades.…”

Section: Whole-cell Cascade Biotransformations Using Microbial Epoxid...mentioning

confidence: 99%

Epoxide Hydrolases: Multipotential Biocatalysts

Bučko

Kaniaková

Hronská

et al. 2023

IJMS

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Epoxide hydrolases are attractive and industrially important biocatalysts. They can catalyze the enantioselective hydrolysis of epoxides to the corresponding diols as chiral building blocks for bioactive compounds and drugs. In this review article, we discuss the state of the art and development potential of epoxide hydrolases as biocatalysts based on the most recent approaches and techniques. The review covers new approaches to discover epoxide hydrolases using genome mining and enzyme metagenomics, as well as improving enzyme activity, enantioselectivity, enantioconvergence, and thermostability by directed evolution and a rational design. Further improvements in operational and storage stabilization, reusability, pH stabilization, and thermal stabilization by immobilization techniques are discussed in this study. New possibilities for expanding the synthetic capabilities of epoxide hydrolases by their involvement in non-natural enzyme cascade reactions are described.

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Section: Whole-cell Cascade Biotransformations Using Microbial Epoxid...mentioning

confidence: 99%

Epoxide Hydrolases: Multipotential Biocatalysts

Bučko

Kaniaková

Hronská

et al. 2023

IJMS

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“…[4] Oxidative enzymes have also been studied in combination with other bio-or chemo-catalysts for the synthesis of a wide variety of high-value chemicals. [5] By developing these reactions in cascade manner, unstable intermediates can be converted into the final products without any purification step, contributing to reduce the waste production and energy consumption through sustainable overall processes. [6] Among oxidative enzymes, laccases (EC 1.10.3.2) have gained increasing attention regarding traditional chemical oxidations, owing to their action under mild reaction conditions and specificity towards phenolic compounds as natural substrates.…”

Section: Introductionmentioning

confidence: 99%

Laccases from Pleurotus ostreatus Applied to the Oxidation of Furfuryl Alcohol for the Synthesis of Key Compounds for Polymer Industry

Cascelli

Lettera

Sannia³

et al. 2023

ChemSusChem

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Laccases are oxidative enzymes with high synthetic potential. In this work, their value in biocatalysis is shown through the green and selective oxidation of furfuryl alcohol into furfural with the aid of mediators. The influence of different parameters, such as pH, enzyme/mediator composition, buffer type, cosolvent tolerance, and reaction times, is investigated. Under the optimal conditions, 20 mol % of TEMPO as mediator and 5.8 U mL À 1 of laccases POXC and POXA1b from Pleurotus ostreatus, quantitative production of furfural is attained after 16 h. POXC laccase stands out for its ability to catalyze the reaction at pH 6.5, whereas POXA1b is notable for its high stability. Furfural conversions reach excellent values (95 %) after 72 h using only 5 mol % of TEMPO at 100 mM. Furthermore, furfuryl alcohol bioamination is achieved by employing the amine transaminase from Chromobacterium violaceum, providing furfuryl amine, a key compound for the polymer industry, through a one-pot sequential approach.

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“…11 SOI was shown to be enantioretentive for the isomerization of (S)-2-phenylpropylene oxide to give the corresponding (S)-2phenylpropionaldehyde in 95% ee 13 and was used in biocatalytic cascades to produce chiral alcohols, amines, and acids. 12,13,16,19 Studies using deuterated epoxides and transmethyl substituted epoxides suggested that the rearrangement mechanism of SOI involves a regioselective and stereospecific 1,2-migration. 14 The key reaction in the proposed chemoenzymatic synthesis is the enantioretentive isomerization of (S)-2-arylpropylene oxides to (S)-2-arylpropionaldehydes.…”

Section: ■ Introductionmentioning

confidence: 99%

“…SOI (EC 5.3.99.7) has recently been receiving increased attention for the Meinwald rearrangement of epoxides to aldehydes − and was characterized as an integral membrane enzyme ,, with a high natural catalytic efficiency of 4.6 × 10 6 M –1 s –1 toward styrene oxide . SOI was shown to be enantioretentive for the isomerization of ( S )-2-phenylpropylene oxide to give the corresponding ( S )-2-phenylpropionaldehyde in 95% ee and was used in biocatalytic cascades to produce chiral alcohols, amines, and acids. ,,, Studies using deuterated epoxides and trans -methyl substituted epoxides suggested that the rearrangement mechanism of SOI involves a regioselective and stereospecific 1,2-migration …”

Section: Introductionmentioning

confidence: 99%

Engineering of Styrene Oxide Isomerase for Enhanced Production of 2-Arylpropionaldehydes: Chemoenzymatic Synthesis of (S)-Profens

et al. 2023

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(S)-Arylpropionic acids are the pharmacologically active enantiomers of profen drugs that are challenging to synthesize chemically. Here, we report a chemoenzymatic synthesis of (S)-profens from alkenes involving styrene oxide isomerase (SOI)-catalyzed enantioretentive Meinwald-type isomerization of epoxides to aldehydes. This success relies on the engineering of SOI to accept larger substrates with enhanced activity for the rate-limiting isomerization step using a multi-Harmony analysis to guide directed evolution, which represents the first successful rational-based evolution of a membrane-associated enzyme without structural information. The engineered SOI-F35A/A131Y demonstrated 10.5-fold improvement in catalytic efficiency compared to wild-type SOI and was successfully combined in a cascade with aldehyde dehydrogenase to produce four (S)-profens from chemically derived (S)-epoxides in 83–89% yield and 90–94% ee. This work represents a simple and cleaner route to synthesize (S)-profens from alkenes, and the engineered SOI can be useful to produce other types of chiral molecules.

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Recent developments in oxidative biocatalytic cascades

Cited by 8 publications

References 51 publications

Epoxide Hydrolases: Multipotential Biocatalysts

Epoxide Hydrolases: Multipotential Biocatalysts

Laccases from Pleurotus ostreatus Applied to the Oxidation of Furfuryl Alcohol for the Synthesis of Key Compounds for Polymer Industry

Engineering of Styrene Oxide Isomerase for Enhanced Production of 2-Arylpropionaldehydes: Chemoenzymatic Synthesis of (S)-Profens

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