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Efficient enzymatic acrylation through transesterification at controlled water activity

Nordblad, Mathias LU and Adlercreutz, Patrick LU (2008) In Biotechnology and Bioengineering 99(6). p.1518-1524
Abstract
Enzymatic acrylation is a process of potentially strong interest to the chemical industry. Direct esterification involving acrylic acid is unfortunately rather slow, with inhibition phenomena appearing at high acid concentrations. In the present study the acrylation of I-octanol catalyzed by immobilized Candida antarctica lipase B (Novozym (R) 435) was shown to be as much as an order of magnitude faster when ethyl acrylate served as the donor of the acrylic group. Water activity is a key parameter for optimizing the rate of ester synthesis. The optimum water activity for the esterification of octanol by acrylic acid was found to be 0.75, that for its esterification by propionic acid to be 0.45 and the transesterification involving ethyl... (More)
Enzymatic acrylation is a process of potentially strong interest to the chemical industry. Direct esterification involving acrylic acid is unfortunately rather slow, with inhibition phenomena appearing at high acid concentrations. In the present study the acrylation of I-octanol catalyzed by immobilized Candida antarctica lipase B (Novozym (R) 435) was shown to be as much as an order of magnitude faster when ethyl acrylate served as the donor of the acrylic group. Water activity is a key parameter for optimizing the rate of ester synthesis. The optimum water activity for the esterification of octanol by acrylic acid was found to be 0.75, that for its esterification by propionic acid to be 0.45 and the transesterification involving ethyl acrylate to be fastest at a water activity of 0.3. The reasons for these differences in optimum water activity are discussed in terms of enzyme specificity, substrate solvation, and mass transfer effects. (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
acrylate synthesis, lipase, ethyl acrylate, water activity
in
Biotechnology and Bioengineering
volume
99
issue
6
pages
1518 - 1524
publisher
John Wiley & Sons
external identifiers
  • wos:000254211700025
  • scopus:41049099710
ISSN
1097-0290
DOI
10.1002/bit.21706
language
English
LU publication?
yes
id
27e988e2-59eb-4210-a3bf-546b715852b0 (old id 1185163)
date added to LUP
2008-09-02 16:27:04
date last changed
2017-01-01 04:42:08
@article{27e988e2-59eb-4210-a3bf-546b715852b0,
  abstract     = {Enzymatic acrylation is a process of potentially strong interest to the chemical industry. Direct esterification involving acrylic acid is unfortunately rather slow, with inhibition phenomena appearing at high acid concentrations. In the present study the acrylation of I-octanol catalyzed by immobilized Candida antarctica lipase B (Novozym (R) 435) was shown to be as much as an order of magnitude faster when ethyl acrylate served as the donor of the acrylic group. Water activity is a key parameter for optimizing the rate of ester synthesis. The optimum water activity for the esterification of octanol by acrylic acid was found to be 0.75, that for its esterification by propionic acid to be 0.45 and the transesterification involving ethyl acrylate to be fastest at a water activity of 0.3. The reasons for these differences in optimum water activity are discussed in terms of enzyme specificity, substrate solvation, and mass transfer effects.},
  author       = {Nordblad, Mathias and Adlercreutz, Patrick},
  issn         = {1097-0290},
  keyword      = {acrylate synthesis,lipase,ethyl acrylate,water activity},
  language     = {eng},
  number       = {6},
  pages        = {1518--1524},
  publisher    = {John Wiley & Sons},
  series       = {Biotechnology and Bioengineering},
  title        = {Efficient enzymatic acrylation through transesterification at controlled water activity},
  url          = {http://dx.doi.org/10.1002/bit.21706},
  volume       = {99},
  year         = {2008},
}