Mass transfer limitation as a tool to enhance the enantiomeric excess in the enzymatic synthesis of chiral cyanohydrins

Gerrits, Pieter Jan; Willeman, W. F.; Straathof, Adrie J. J.; Heijnen, Joseph J.; Brussee, Johannes; Gen, A. Van Der

doi:10.1016/s1381-1177(01)00014-5

Cited by 38 publications

(36 citation statements)

References 16 publications

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“…-Undesired consecutive or side reactions can be avoided (Gerrits et al, 2001;Villela Filho et al, 2003).…”

Section: Enzyme Reactions Using Non-conventional Mediamentioning

confidence: 99%

“…This makes process design more complex (Halling, 1994) and may result in mass transfer limitation which lowers the productivity (Baldascini et al, 2001). However, in certain cases mass transfer limitation can also be favorable, for example in order to suppress a chemical side reaction (Gerrits et al, 2001;Willeman et al, 2002a). Mass transfer limitation can be avoided by decreasing the enzyme concentration or by increasing agitation or interfacial area (Straathof, 2003).…”

Section: Coupling Of Enzyme and Mass Transfer Kineticsmentioning

confidence: 99%

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Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Zavrel

Schmidt

Michalik

et al. 2007

Journal of Biotechnology

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“…-Undesired consecutive or side reactions can be avoided (Gerrits et al, 2001;Villela Filho et al, 2003).…”

Section: Enzyme Reactions Using Non-conventional Mediamentioning

confidence: 99%

Section: Coupling Of Enzyme and Mass Transfer Kineticsmentioning

confidence: 99%

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Zavrel

Schmidt

Michalik

et al. 2007

Journal of Biotechnology

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“…This can be a result of changes in the concentration of substrates and products [3][4][5][6] in the vicinity of the catalyst, direct interactions of small amounts of dissolved solvent with the catalyst [7], or interaction of the catalyst with the interface between aqueous and organic phase [7][8][9][10]. These parameters can either affect activity/productivity or selectivity of the biocatalyzed reaction [3][4][5][6][7][8][9] or influence the stability of the catalyst [6,10].…”

mentioning

confidence: 99%

“…These parameters can either affect activity/productivity or selectivity of the biocatalyzed reaction [3][4][5][6][7][8][9] or influence the stability of the catalyst [6,10]. The activity of many lipases, for instance, is considerably enhanced at interfaces whereas the same interaction may deactivate other enzymes [6,10].…”

mentioning

confidence: 99%

“…Emulsion systems are therefore not applicable for a thorough characterization of biphasic systems, in contrast to studies that used systems with two defined and distinguishable liquid phases. Most examples are concerned with the interactions between biocatalyst and solvent phase, either revealing inactivation at the interface [6,10] or contrariwise interfacial activity…”

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confidence: 99%

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Biphasic mini‐reactor for characterization of biocatalyst performance

Wittenboer

Schmidt

Müller

et al. 2009

Biotechnology Journal

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Biphasic reaction media are extending the scope of technical biocatalysis. Thorough investigation of the factors affecting catalyst performance under these conditions is of key importance for the successful implementation of catalytic processes. Here, we present a reactor setup suitable for comprehensive systematic characterization and optimization of biocatalyzed reactions in biphasic systems with distinct phases. It is distinguished by small volumes allowing reproducible experimentation with minimum amounts of solvent and catalyst. The interfacial area is kept constant and independent stirring of both phases is allowed in order to minimize superimposing effects. Evaporation of low‐volatile organic solvents is prevented by use of airtight construction. The broad applicability of this mini‐reactor is demonstrated with regard to determination of mass transfer, enzyme productivity, and enzyme stability in both batch and continuous mode.

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Enzymatic C‐C Bond Formation, Asymmetric

Kara¹,

Liese²

2010

Encyclopedia of Industrial Biotechnology

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The environmental awareness has grown during the past years focusing on efficient utilization of energy, elimination of waste and avoidance of toxic and/or hazardous reagents.Biocatalysis fulfills the requirement of “green chemistry”; since enzymes are biodegradable catalysts which can effectively catalyze the reactions under mild conditions(ambient temperature, no need for high pressure, no extreme pH, no toxic solvents and no heavy metal catalysts).C–C bond formation reactions are fundamental to all of organic chemistry, and enzymes show promise for use in this field. A variety of versatile building blocks in organic and pharmaceutical chemistry can be synthesized by biocatalysts. In comparison to available chemical routes enzymes also provide chemo‐, regio‐, and stereoselective catalysis. Different enzyme classes are applied in the field of C–C bond formation to synthesize complex, aldol reactions, and cyanohydrin formations. Few applications are also found in ketol‐ and aldol transfer reactions. Furthermore, promiscuous activity of lipases can be applied in C–C bond formation reactions.

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Mass transfer limitation as a tool to enhance the enantiomeric excess in the enzymatic synthesis of chiral cyanohydrins

Cited by 38 publications

References 16 publications

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Biphasic mini‐reactor for characterization of biocatalyst performance

Enzymatic C‐C Bond Formation, Asymmetric

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