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:
https://lup.lub.lu.se/record/1185163
- author
- Nordblad, Mathias
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2008
- 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 Inc.
- 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
- 2016-04-01 11:57:26
- date last changed
- 2022-01-26 20:43:56
@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}},
keywords = {{acrylate synthesis; lipase; ethyl acrylate; water activity}},
language = {{eng}},
number = {{6}},
pages = {{1518--1524}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Biotechnology and Bioengineering}},
title = {{Efficient enzymatic acrylation through transesterification at controlled water activity}},
url = {{http://dx.doi.org/10.1002/bit.21706}},
doi = {{10.1002/bit.21706}},
volume = {{99}},
year = {{2008}},
}