Enantioselective hydrolysis of styrene oxide with the epoxide hydrolase of Sphingomonas sp. HXN-200

Liu, Zeya; Michel, Johannes Ehrenreich Josef; Wang, Zunsheng; Witholt, Bernard; Li, Zhi

doi:10.1016/j.tetasy.2005.11.018

Cited by 40 publications

(28 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…VLB120 was selected since its extensive application in chiral epoxide synthesis. − For the second hydrolysis step, SpEH from Sphingomonas sp. HXN-200 was selected because of its remarkable activity in the enantioselective hydrolysis of ( S )-styrene oxides to ( S )-diols in high ee. − For the third oxidation step, an NAD + -dependent ( S )-selective polyol dehydrogenase (GoSCR) from Gluconobacter oxydans was employed for the regio- and enantioselective oxidation of ( S )-diol to α-hydroxy ketone . Then, an in situ cofactor regeneration system was formed by SMO-catalyzed epoxidation (NADH to NAD + ) and GoSCR-catalyzed oxidation (NAD + to NADH) (Scheme ).…”

Section: Resultsmentioning

confidence: 99%

Cascade Biocatalysis for Regio- and Stereoselective Aminohydroxylation of Styrenyl Olefins to Enantiopure Arylglycinols

Zhang

Yang

Dong

et al. 2020

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

Chiral β-amino alcohols are privileged scaffolds frequently found in pharmaceutically active molecules and natural products. Aminohydroxylation of olefins is one of the most powerful strategies to access chiral vicinal amino alcohols. However, the direct regio-and stereoselective aminohydroxylation of olefins to unprotected enantioenriched β-amino alcohols remains a longstanding challenge. Herein, we report that a novel one-pot four-enzyme [styrene monooxygenase (SMO)/epoxide hydrolase (EH)/ alcohol dehydrogenase (ADH)/ω-transaminase (TA)] biocatalytic cascade efficiently catalyzes the direct transformation of readily available styrenyl olefins into unprotected 2-amino-2-phenyl ethanols in good yields and excellent enantioselectivity. In vitro cascade biocatalysis aminohydroxylation of styrenyl olefins was first investigated by the combined four enzymes (SMO/EH/ADH/TA) with a trace amount of NADH (0.02 mM) and pyridoxal-5′-phosphate (0.1 mM), affording both enantiomers of β-amino alcohols 5a−j in 13.9−98.7% conversions and 86−99% ee. Whole-cell-based cascade biocatalysis was achieved by using the constructed recombinant Escherichia coli pairwise combinations and single tailor-made whole-cell biocatalyst without an additional NADH cofactor; (R)-and (S)-β-amino alcohols 5a−j could be obtained in 14.6−99.7% conversions and 86−99% ee. Moreover, the preparative experiments of this new cascade biocatalysis were demonstrated by the single tailor-made whole-cell biocatalyst [E. coli (CGS-DEM) and E. coli (CGS-DEB)] with the substrates 1a−b and 1h in an aqueous-organic two-phase system, affording chiral βamino alcohols [(R)-or (S)-5a−b, h] in good yields (50.9−64.3%) and excellent ee (>99%).

show abstract

Section: Resultsmentioning

confidence: 99%

Cascade Biocatalysis for Regio- and Stereoselective Aminohydroxylation of Styrenyl Olefins to Enantiopure Arylglycinols

Zhang

Yang

Dong

et al. 2020

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

show abstract

“…To demonstrate this novel concept of using the stable organic–inorganic capsules for enzyme immobilization, we chose epoxide hydrolase SpEH as the model enzyme (Chang et al, ; Jia et al, ; Liu et al, ; Wu et al, ). SpEH catalyzes the regio‐ and enantio‐selective hydrolysis of several racemic epoxides to give the enantiopure epoxides in high ee and good yield (Jia et al, ; Liu et al, ; Wu et al, ), and it also catalyzes the enantioselective hydrolysis of some meso‐epoxides to produce the corresponding diols in high yield and good ee (Chang et al, ; Wu et al, ). Development of active and recyclable immobilized SpEH could significantly reduce the enzyme cost and enhance the operational stability, thus improving the process economics for the preparation of the useful and valuable chiral epoxides and diols.…”

Section: Resultsmentioning

confidence: 99%

Encapsulation of enzyme via one‐step template‐free formation of stable organic–inorganic capsules: A simple and efficient method for immobilizing enzyme with high activity and recyclability

Huang

Goldman

et al. 2015

Biotech & Bioengineering

Self Cite

View full text Add to dashboard Cite

Enzyme encapsulation is a simple, gentle, and general method for immobilizing enzyme, but it often suffers from one or more problems regarding enzyme loading efficiency, enzyme leakage, mechanical stability, and recyclability. Here we report a novel, simple, and efficient method for enzyme encapsulation to overcome these problems by forming stable organic-inorganic hybrid capsules. A new, facile, one-step, and template-free synthesis of organic-inorganic capsules in aqueous phase were developed based on PEI-induced simultaneous interfacial self-assembly of Fmoc-FF and polycondensation of silicate. Addition of an aqueous solution of Fmoc-FF and sodium silicate into an aqueous solution of PEI gave a new class of organic-inorganic hybrid capsules (FPSi) with multi-layered structure in high yield. The capsules are mechanically stable due to the incorporation of inorganic silica. Direct encapsulation of enzyme such as epoxide hydrolase SpEH and BSA along with the formation of the organic-inorganic capsules gave high yield of enzyme-containing capsules (∼1.2 mm in diameter), >90% enzyme loading efficiency, high specific enzyme loading (158 mg protein g(-1) carrier), and low enzyme leakage (<3% after 48 h incubation). FPSi-SpEH capsules catalyzed the hydrolysis of cyclohexene oxide to give (1R, 2R)-cyclohexane-1,2-diol in high yield and concentration, with high specific activity (6.94 U mg(-1) protein) and the same high enantioselectivity as the free enzyme. The immobilized SpEH demonstrated also excellent operational stability and recyclability: retaining 87% productivity after 20 cycles with a total reaction time of 80 h. The new enzyme encapsulation method is efficient, practical, and also better than other reported encapsulation methods.

show abstract

“…An increase in E-value in an n-hexane-containing two-phase reaction system was determined for the EHmediated enantioselective hydrolysis of styrene oxide using a freeze-dried cell-free extract from Sphingomonas sp. (Liu et al, 2006).…”

Section: Eh-catalyzed Reactions In Organic Solvent-or Ionic Liquid-co...mentioning

confidence: 99%

Epoxide Hydrolases and their Application in Organic Synthesis

2016

View full text Add to dashboard Cite

c h a p t e r 8 INTRODUCTIONOrganic chemists have become interested in enzymes as catalysts due to their high efficiencies and specificities. Moreover, recent progress in molecular biology and enzyme-related research areas enabled and simplified the production and purifica tion of recombinant enzymes in large quantities and their engineering toward tailormade biocatalysts using straightforward mutagenesis and screening techniques. This is also true for epoxide hydrolases (EHs), as evidenced by the many published research papers about the synthetic applications of naturally occurring or engi neered EHs. EHs catalyze the opening of oxirane rings, generating a vicinal diol as the final product ( Figure 8.1). From a synthetic chemistry point of view, the most valuable EHs are those with either (i) high enantioselectivities or (ii) a combination of low enantio preference with a high level of enantioconvergence. While the former generate enan tiopure epoxides with a maximum yield of 50% in a kinetic resolution process, the latter produce ideally an enantiopure diol product with a theoretical yield of 100%. Thus, EHs provide convenient access to enantiopure epoxides or diols from racemic epoxides. Furthermore, the enantiopure diols can then often be chemically trans formed back to the corresponding epoxides with no effect on the enantiomeric excess (ee). High values of enantioselectivity or enantioconvergence are a consequence of particular enzyme-substrate interactions, which can be modulated by specific reac tion conditions or through the exchange of specific amino acids of the biocatalyst. The final stereochemical outcome of an EH-catalyzed reaction depends solely on the regioselectivity coefficients, which determine the absolute configuration and the ee of the diol product when the reaction reaches 100% conversion. During the reaction, the oxirane ring of each enantiomer is often attacked at either carbon atom, resulting in a mixture of diol enantiomers (Figure 8.2). Unfortunately, several authors used the product-derived E-value, E P (calculated from c and ee P using Sih's equation; see Ref.[1]) for characterizing the stereochemistry of the diol formation of an EH-mediated hydrolysis reaction [2,3]. This is wrong and misleading for epoxide-opening reac tions since there are two possible positions of attack for each oxirane enantiomer. The ideal enantioconvergent EH leads to deracemization of a racemic mixture of an epox ide and exhibits reversed regioselectivity for either substrate enantiomer, that is,

show abstract

Enantioselective hydrolysis of styrene oxide with the epoxide hydrolase of Sphingomonas sp. HXN-200

Cited by 40 publications

References 36 publications

Cascade Biocatalysis for Regio- and Stereoselective Aminohydroxylation of Styrenyl Olefins to Enantiopure Arylglycinols

Cascade Biocatalysis for Regio- and Stereoselective Aminohydroxylation of Styrenyl Olefins to Enantiopure Arylglycinols

Encapsulation of enzyme via one‐step template‐free formation of stable organic–inorganic capsules: A simple and efficient method for immobilizing enzyme with high activity and recyclability

Epoxide Hydrolases and their Application in Organic Synthesis

Contact Info

Product

Resources

About