Stability, activity, and selectivity of benzaldehyde lyase in supercritical fluids

Natalia, Dessy; Greiner, Lasse; Leitner, Walter; Ansorge‐Schumacher, Marion B.

doi:10.1016/j.supflu.2011.11.025

Cited by 12 publications

(5 citation statements)

References 35 publications

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“…Similar pronounced effects on the activity and stereoselectivity of BAL were observed by the group of Ansorge-Schumacher, who studied this enzyme in supercritical fluids [100].…”

Section: Influence Of Reaction Conditions On Chemoselectivity and Stesupporting

confidence: 78%

Engineering stereoselectivity of ThDP-dependent enzymes

Hailes

Rother

Müller

et al. 2013

FEBS J

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Thiamine diphosphate-dependent enzymes are broadly distributed in all organisms, and they catalyse a broad range of C-C bond forming and breaking reactions. Enzymes belonging to the structural families of decarboxylases and transketolases have been particularly well investigated concerning their substrate range, mechanism of stereoselective carboligation and carbolyase reaction. Both structurally different enzyme families differ also in stereoselectivity: enzymes from the decarboxylase family are predominantly R-selective, whereas those from the transketolase family are S-selective. In recent years a key focus of our studies has been on stereoselective benzoin condensation-like 1,2-additions. Meanwhile, several S-selective variants of pyruvate decarboxylase, benzoylformate decarboxylase and 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPH-CHC) synthase as well as R-selective transketolase variants were created that allow access to a broad range of enantiocomplementary a-hydroxyketones and a,a′-dihydroxyketones. This review covers recent studies and the mechanistic understanding of stereoselective C-C bond forming thiamine diphosphate-dependent enzymes, which has been guided by structure-function analyses based on mutagenesis studies and from influences of different substrates and organic co-solvents on stereoselectivity.

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“…Similar pronounced effects on the activity and stereoselectivity of BAL were observed by the group of Ansorge-Schumacher, who studied this enzyme in supercritical fluids [100].…”

Section: Influence Of Reaction Conditions On Chemoselectivity and Stesupporting

confidence: 78%

Engineering stereoselectivity of ThDP-dependent enzymes

Hailes

Rother

Müller

et al. 2013

FEBS J

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“…Natalia et al [95] studied the selectivity of benzaldehyde lyase (BAL) in four supercritical fluids (carbon dioxide, fluoroform, ethane, and sulphur hexafluoride), and found that the enzyme enantioselectivity was almost racemic with the highest enantiomeric excess for fluoroform (40%). However, when excess water was added to the supercritical fluids, the enantiomeric excess increased up to more than 90% for fluoroform, ethane, and sulphur hexafluoride, indicating that water activity was a main factor in the selectivity.…”

Section: Effects Of Pressure and Temperature On The Structure And Actmentioning

confidence: 99%

Enzyme Stability and Activity in Non-Aqueous Reaction Systems: A Mini Review

et al. 2016

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Abstract:Enormous interest in biocatalysis in non-aqueous phase has recently been triggered due to the merits of good enantioselectivity, reverse thermodynamic equilibrium, and no water-dependent side reactions. It has been demonstrated that enzyme has high activity and stability in non-aqueous media, and the variation of enzyme activity is attributed to its conformational modifications. This review comprehensively addresses the stability and activity of the intact enzymes in various non-aqueous systems, such as organic solvents, ionic liquids, sub-/super-critical fluids and their combined mixtures. It has been revealed that critical factors such as Log P, functional groups and the molecular structures of the solvents define the microenvironment surrounding the enzyme molecule and affect enzyme tertiary and secondary structure, influencing enzyme catalytic properties. Therefore, it is of high importance for biocatalysis in non-aqueous media to elucidate the links between the microenvironment surrounding enzyme surface and its stability and activity. In fact, a better understanding of the correlation between different non-aqueous environments and enzyme structure, stability and activity can contribute to identifying the most suitable reaction medium for a given biotransformation.

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“…The work of Fricks et al indicated that the horseradish peroxidase (HRP) treatment in CO 2 promotes a significant decrease in the enzyme stability, whereas HRP showed good stability in propane [43]. In the study of Synthesis of (R)-1,2-di(furan-2-yl)-2-hydroxyethanone in supercritical fluids using benzaldehyde lyase, non-carbon dioxide supercritical fluids such as propane give better results in view of stability [18].…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, the utility of this scf is limited due to its undesirable effects on the enzyme stability. It has been shown in recent experimental observations that other compressed gases, like near-critical propane; seem also to be adequate for enzymecatalyzed reactions [15][16][17][18][19][20][21][22][23][24]. In contrast to supercritical conditions of CO 2 , enzymatic reactions are commonly conducted in nearcritical propane in which propane behaves like a conventional liquid.…”

Section: Introductionmentioning

confidence: 99%