Advanced

Effects of solvent, water activity and temperature on lipase and hydroxynitrile lyase enantioselectivity

Persson, Mattias LU ; Costes, D; Wehtje, Ernst LU and Adlercreutz, Patrick LU (2002) In Enzyme and Microbial Technology 30(7). p.916-923
Abstract
The influence of the reaction conditions on the enantioselectivity of reactions catalysed by lipases or hydroxynitrile leases (HNLs) in organic solvents was investigated. The lipases catalysed kinetic resolution of chiral secondary alcohol, or chiral carboxylic acids and the HNLs catalysed asymmetric addition of hydrogen cyanide to aldehydes. The temperature effects on enantioselectivity, were studied in detail. From measurements of the enantiomeric ratio (C) at different temperatures the activation parameters DeltaDeltaH(#) and DeltaDeltaS(#) were determined. In the lipase-catalysed reactions the enthalpic and entropic effects on E always counteracted, while in a few of the HNL-catalysed reactions, DeltaDeltaH(#) and DeltaDeltaS(#) had... (More)
The influence of the reaction conditions on the enantioselectivity of reactions catalysed by lipases or hydroxynitrile leases (HNLs) in organic solvents was investigated. The lipases catalysed kinetic resolution of chiral secondary alcohol, or chiral carboxylic acids and the HNLs catalysed asymmetric addition of hydrogen cyanide to aldehydes. The temperature effects on enantioselectivity, were studied in detail. From measurements of the enantiomeric ratio (C) at different temperatures the activation parameters DeltaDeltaH(#) and DeltaDeltaS(#) were determined. In the lipase-catalysed reactions the enthalpic and entropic effects on E always counteracted, while in a few of the HNL-catalysed reactions, DeltaDeltaH(#) and DeltaDeltaS(#) had opposite sign, and therefore the effects cooperated to give high E values (-RTInE = DeltaDeltaG(#) = DeltaDeltaH(#) - TDeltaDeltaS(#)). In all the HNL-catalysed reactions and most of the lipase-catalysed ones, the enantioselectivity increased with decreasing reaction temperature. However, in one of the lipase-catalysed reactions, the enantioselectivity decreased with decreasing temperature. The theoretical background of these observations wars discussed. In the HNL-catalysed reactions, the enantioselectivity increased with increasing water content up to water saturation, while in the lipase-catalysed reactions the opposite trend was found in one case and in the others no significant effect was observed. Solvent mixtures of diisopropylether and hexane were used to obtain solvents with different log P values. The log P value of the solvent did not influence the enantioselectivity in the HNL-catalysed reactions. while the enantioselectivity increased with increasing log P value in two of the lipase-catalysed reactions. The reaction temperature was shown to be a very useful way to influence enzyme selectivity and the effects obtained could be rationalised. The influence of the reaction medium (solvent and water activity) is much more difficult to rationalise and predict. (C) 2002 Elsevier Science Inc. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
temperature, hydroxynitrile lyase, enantioselectivity, lipase, water, activity, organic solvent
in
Enzyme and Microbial Technology
volume
30
issue
7
pages
916 - 923
publisher
Elsevier
external identifiers
  • wos:000175961300013
  • scopus:0037018905
ISSN
0141-0229
DOI
10.1016/S0141-0229(02)00033-9
language
English
LU publication?
yes
id
863763d2-0124-469c-a85a-def9adb91a2d (old id 336099)
date added to LUP
2007-11-08 14:04:56
date last changed
2017-09-03 03:55:38
@article{863763d2-0124-469c-a85a-def9adb91a2d,
  abstract     = {The influence of the reaction conditions on the enantioselectivity of reactions catalysed by lipases or hydroxynitrile leases (HNLs) in organic solvents was investigated. The lipases catalysed kinetic resolution of chiral secondary alcohol, or chiral carboxylic acids and the HNLs catalysed asymmetric addition of hydrogen cyanide to aldehydes. The temperature effects on enantioselectivity, were studied in detail. From measurements of the enantiomeric ratio (C) at different temperatures the activation parameters DeltaDeltaH(#) and DeltaDeltaS(#) were determined. In the lipase-catalysed reactions the enthalpic and entropic effects on E always counteracted, while in a few of the HNL-catalysed reactions, DeltaDeltaH(#) and DeltaDeltaS(#) had opposite sign, and therefore the effects cooperated to give high E values (-RTInE = DeltaDeltaG(#) = DeltaDeltaH(#) - TDeltaDeltaS(#)). In all the HNL-catalysed reactions and most of the lipase-catalysed ones, the enantioselectivity increased with decreasing reaction temperature. However, in one of the lipase-catalysed reactions, the enantioselectivity decreased with decreasing temperature. The theoretical background of these observations wars discussed. In the HNL-catalysed reactions, the enantioselectivity increased with increasing water content up to water saturation, while in the lipase-catalysed reactions the opposite trend was found in one case and in the others no significant effect was observed. Solvent mixtures of diisopropylether and hexane were used to obtain solvents with different log P values. The log P value of the solvent did not influence the enantioselectivity in the HNL-catalysed reactions. while the enantioselectivity increased with increasing log P value in two of the lipase-catalysed reactions. The reaction temperature was shown to be a very useful way to influence enzyme selectivity and the effects obtained could be rationalised. The influence of the reaction medium (solvent and water activity) is much more difficult to rationalise and predict. (C) 2002 Elsevier Science Inc. All rights reserved.},
  author       = {Persson, Mattias and Costes, D and Wehtje, Ernst and Adlercreutz, Patrick},
  issn         = {0141-0229},
  keyword      = {temperature,hydroxynitrile lyase,enantioselectivity,lipase,water,activity,organic solvent},
  language     = {eng},
  number       = {7},
  pages        = {916--923},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Effects of solvent, water activity and temperature on lipase and hydroxynitrile lyase enantioselectivity},
  url          = {http://dx.doi.org/10.1016/S0141-0229(02)00033-9},
  volume       = {30},
  year         = {2002},
}