Diffusion limitation causes decreased enantioselectivity of esterification of 2-butanol by immobilized Candida antarctica lipase B

Journal article (2001)

Authors

MJJ Litjens OLD BT/Cell Systems Engineering
Adrie J.J. Straathof BT/Bioprocess Engineering - AS
JA Jongejan BT/Enzymology
J.J. Heijnen OLD BT/Cell Systems Engineering
Research Group
BT/Bioprocess Engineering (AS) (TU Delft)
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Published Date

2001

Language

English

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Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Bioprocess Engineering

Abstract

Diffusion limitation in immobilized enzyme particles may decrease the performance of kinetic resolution processes. In this paper a standard reaction plus diffusion model approach, based on homogeneous enzyme distribution, is used to verify experimentally the influence of the particle diameter on the observed enantioselectivity. This is done for a commercial preparation of immobilized Candida antarctica lipase B in the kinetic resolution of racemic 2-butanol by esterification with vinyl butyrate in heptane. For immobilized enzyme particles with particle diameters ranging from 355-710 μm the apparent enantiomeric ratio is constant at Eapp = 2.5, while for ground particles with a particle diameter of 1 μm the intrinsic enantiomeric ratio is E = 4.4. This clear example of the influence of diffusion limitation on the observed enantioselectivity can not be described quantitatively in a straightforward way, because the enzyme seems to be present as a layer in the carrier particles.