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Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions

Ma, L; Persson, Mattias LU and Adlercreutz, Patrick LU (2002) In Enzyme and Microbial Technology 31(7). p.1024-1029
Abstract
The water activity dependence of lipase kinetics in organic media was evaluated using lipases from Rhizopus oryzae and Candida rugosa immobilised on polypropene EP-100. The conversion studied was the transesterification of ethyl decanoate to hexyl decanoate with hydrolysis to decanoic acid as competing reaction. The reactions were carried out at controlled water activity in diisopropyl ether. Substrate inhibition was observed at hexanol concentrations of 100 mM or higher. The Rhizopus lipase expressed the highest activity and the best selectivity for transesterification at the lowest water activity (a(w) = 0.06). The Candida lipase expressed the highest transesterification/hydrolysis ratio at a(w) = 0.11 and the highest total activity at... (More)
The water activity dependence of lipase kinetics in organic media was evaluated using lipases from Rhizopus oryzae and Candida rugosa immobilised on polypropene EP-100. The conversion studied was the transesterification of ethyl decanoate to hexyl decanoate with hydrolysis to decanoic acid as competing reaction. The reactions were carried out at controlled water activity in diisopropyl ether. Substrate inhibition was observed at hexanol concentrations of 100 mM or higher. The Rhizopus lipase expressed the highest activity and the best selectivity for transesterification at the lowest water activity (a(w) = 0.06). The Candida lipase expressed the highest transesterification/hydrolysis ratio at a(w) = 0.11 and the highest total activity at a(w) = 0.53. Several glycosidases previously tested under conditions similar to those used here expressed both maximal total activity and the best selectivity at water activities close to 1.0. The water activity dependence of the lipases is thus fundamentally different from that of glycosidases and it is a major part of the reason why lipases are more suited for transferase-type reactions than the glycosidases. (C) 2002 Elsevier Science Inc. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lipase catalysis, hydrolases, transesterification, water activity
in
Enzyme and Microbial Technology
volume
31
issue
7
pages
1024 - 1029
publisher
Elsevier
external identifiers
  • wos:000179783500014
  • scopus:0037010874
ISSN
0141-0229
DOI
10.1016/S0141-0229(02)00231-4
language
English
LU publication?
yes
id
d7495800-563a-4188-83cb-4405b9c53d5b (old id 321781)
date added to LUP
2007-11-19 12:53:23
date last changed
2017-07-30 03:52:06
@article{d7495800-563a-4188-83cb-4405b9c53d5b,
  abstract     = {The water activity dependence of lipase kinetics in organic media was evaluated using lipases from Rhizopus oryzae and Candida rugosa immobilised on polypropene EP-100. The conversion studied was the transesterification of ethyl decanoate to hexyl decanoate with hydrolysis to decanoic acid as competing reaction. The reactions were carried out at controlled water activity in diisopropyl ether. Substrate inhibition was observed at hexanol concentrations of 100 mM or higher. The Rhizopus lipase expressed the highest activity and the best selectivity for transesterification at the lowest water activity (a(w) = 0.06). The Candida lipase expressed the highest transesterification/hydrolysis ratio at a(w) = 0.11 and the highest total activity at a(w) = 0.53. Several glycosidases previously tested under conditions similar to those used here expressed both maximal total activity and the best selectivity at water activities close to 1.0. The water activity dependence of the lipases is thus fundamentally different from that of glycosidases and it is a major part of the reason why lipases are more suited for transferase-type reactions than the glycosidases. (C) 2002 Elsevier Science Inc. All rights reserved.},
  author       = {Ma, L and Persson, Mattias and Adlercreutz, Patrick},
  issn         = {0141-0229},
  keyword      = {lipase catalysis,hydrolases,transesterification,water activity},
  language     = {eng},
  number       = {7},
  pages        = {1024--1029},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Water activity dependence of lipase catalysis in organic media explains successful transesterification reactions},
  url          = {http://dx.doi.org/10.1016/S0141-0229(02)00231-4},
  volume       = {31},
  year         = {2002},
}