Influence of reaction conditions on the enantioselectivity of biocatalyzed C–C bond formations under high pressure conditions

Kara, Selin; Long, Wei; Berheide, Marco; Peper, Stephanie; Niemeyer, Bernd; Liese, Andreas

doi:10.1016/j.jbiotec.2011.01.020

Cited by 18 publications

(11 citation statements)

References 49 publications

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“…Enzymatic activity determination was carried out according to [ 19 ]: one unit is defined as the amount of enzyme in milligrams transforming 1 mmol benzaldehyde and acetaldehyde to hydroxyl phenylpropanone (HPP) per min in 100 m m phosphate buffer containing 0.5 m m thiamine diphosphate (ThDP) and 2 m m MgCl 2 , 400 m m acetaldehyde and 40 m m benzaldehyde at pH 7.5 and 30 ° C. The tenfold acetaldehyde excess was chosen according to the K m values determined for BFD in previous studies [ 19 ].…”

Section: Enzymatic Assaymentioning

confidence: 99%

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Fagaschewski

Bohne

Kaufhold

et al. 2012

Green Processing and Synthesis

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The downscale of different unit operations for the biocatalytic carboligation of benzaldehyde and acetaldehyde catalyzed by benzoylformate decarboxylase from Pseudomonas putida was investigated. The reactor volume was reduced to 115 μ l thus enabling a substrate and enzyme saving by a factor of 52 in comparison to standard laboratory techniques. Additionally, the successful downscale of membrane based liquid-liquid contactors was shown, which allows, for example, the screening of solvents for extraction as well as the feed of a substrate. Here, comparable volumes as well as residence times were realized, enabling the integration of all three unit operations.

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Section: Enzymatic Assaymentioning

confidence: 99%

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Fagaschewski

Bohne

Kaufhold

et al. 2012

Green Processing and Synthesis

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“…[1][2][3][4] To the development of new tailor-made enzymes for technical applications, studies on the improvement of enzyme activity by changing the physical-chemical conditions (e.g. [1][2][3][4] To the development of new tailor-made enzymes for technical applications, studies on the improvement of enzyme activity by changing the physical-chemical conditions (e.g.…”

Section: Introductionmentioning

confidence: 99%

Combined pressure and cosolvent effects on enzyme activity – a high-pressure stopped-flow kinetic study on α-chymotrypsin

Luong

Winter

2015

Phys. Chem. Chem. Phys.

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We investigated the combined effects of cosolvents and pressure on the hydrolysis of a model peptide catalysed by α-chymotrypsin. The enzymatic activity was measured in the pressure range from 0.1 to 200 MPa using a high-pressure stopped-flow systems with 10 ms time resolution. A kosmotropic (trimethalymine-N-oxide, TMAO) and chaotropic (urea) cosolvent and mixtures thereof were used as cosolvents. High pressure enhances the hydrolysis rate as a consequence of a negative activation volume, ΔV(#), which, depending on the cosolvent system, amounts to -2 to -4 mL mol(-1). A more negative activation volume can be explained by a smaller compression of the ES complex relative to the transition state. Kinetic constants, such as kcat and the Michaelis constant KM, were determined for all solution conditions as a function of pressure. With increasing pressure, kcat increases by about 35% and its pressure dependence by a factor of 1.9 upon addition of 2 M urea, whereas 1 M TMAO has no significant effect on kcat and its pressure dependence. Similarly, KM increases upon addition of urea 6-fold. Addition of TMAO compensates the urea-effect on kcat and KM to some extent. The maximum rate of the enzymatic reaction increases with increasing pressure in all solutions except in the TMAO : urea 1 : 2 mixture, where, remarkably, pressure is found to have no effect on the rate of the enzymatic reaction anymore. Our data clearly show that compatible solutes can easily override deleterious effects of harsh environmental conditions, such as high hydrostatic pressures in the 100 MPa range, which is the maximum pressure encountered in the deep biosphere on Earth.

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“…Increasing attention has been concentrated on enzymatic synthesis in supercritical carbon dioxide (SC‐CO 2 ) for biocatalytic reactions because CO 2 is nontoxic, readily available, inexpensive and easy to remove without leaving residuals in a product matrix. Enzymatic synthesis in SC‐CO 2 has been performed with respect to amidation, esterification, transesterification, carboxylation, acetylation, enantioselection, transglycosylation, reduction and hydrolysis . Many applications of SC‐CO 2 for performing enzyme catalyzed processes have revealed that it is an important sustainable, environmentally friendly and simple approach.…”

Section: Introductionmentioning

confidence: 99%

Effect of sub‐ and super‐critical CO₂ pretreatment on conformation and catalytic properties evaluation of two commercial enzymes of CALB and Lipase PS

Liu

Chen

Wang

2013

J of Chemical Tech & Biotech

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BACKGROUND: It is vitally important to understand the effect of sub-/super-critical CO 2 pretreatment on enzyme conformation and its activity, which should improve the understanding of enzymatic biotransformation applications in nonaqueous media. This study evaluated the effect of sub-/super-critical CO 2 treatment, including pressure (6 and 10 MPa), exposure time (20, 30 and 150 min) and temperature (35 and 40 • C), on the conformation (e.g. 1D, 2D and 3D structures) and catalytic properties (e.g. residual activity, kinetics constants (K m and V max ), activation energies (E α ), thermo-stability and organic solvent tolerance) of two commercial enzymes, CALB and lipase PS in their solution forms.RESULTS: Compared with the blank control, the 1D structure of both treated lipases was unchanged, whereas their 2D and 3D structures were altered to some extent. The highest relative activities were 105% and 116% for CALB and lipase PS, respectively. For CALB, V max /K m value significantly increased, while for lipase PS, V max /K m value was almost constant. Both treated enzymes showed high thermo-stability with recovery of enzyme activity up to 76% and 80%, respectively. Also, both treated enzymes presented high organic solvent tolerance. CONCLUSIONS: It was speculated that 2D, 3D structure alterations were probably responsible for the satisfactory catalytic properties of enzymes treated with sub-/super-critical CO 2 .

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Influence of reaction conditions on the enantioselectivity of biocatalyzed C–C bond formations under high pressure conditions

Cited by 18 publications

References 49 publications

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Combined pressure and cosolvent effects on enzyme activity – a high-pressure stopped-flow kinetic study on α-chymotrypsin

Effect of sub‐ and super‐critical CO₂ pretreatment on conformation and catalytic properties evaluation of two commercial enzymes of CALB and Lipase PS

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Influence of reaction conditions on the enantioselectivity of biocatalyzed C–C bond formations under high pressure conditions

Cited by 18 publications

References 49 publications

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Modular micro reaction engineering for carboligation catalyzed by benzoylformate decarboxylase

Combined pressure and cosolvent effects on enzyme activity – a high-pressure stopped-flow kinetic study on α-chymotrypsin

Effect of sub‐ and super‐critical CO2 pretreatment on conformation and catalytic properties evaluation of two commercial enzymes of CALB and Lipase PS

Contact Info

Product

Resources

About

Effect of sub‐ and super‐critical CO₂ pretreatment on conformation and catalytic properties evaluation of two commercial enzymes of CALB and Lipase PS