Efficient enzymatic acrylation through transesterification at controlled water activity
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 1‐octanol catalyzed b...
Published in: | Biotechnology and Bioengineering |
---|---|
Main Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2007
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/bit.21706 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.21706 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.21706 |
id |
crwiley:10.1002/bit.21706 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/bit.21706 2024-06-02T07:58:07+00:00 Efficient enzymatic acrylation through transesterification at controlled water activity Nordblad, Mathias Adlercreutz, Patrick 2007 http://dx.doi.org/10.1002/bit.21706 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.21706 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.21706 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biotechnology and Bioengineering volume 99, issue 6, page 1518-1524 ISSN 0006-3592 1097-0290 journal-article 2007 crwiley https://doi.org/10.1002/bit.21706 2024-05-03T11:49:52Z 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 1‐octanol catalyzed by immobilized Candida antarctica lipase B (Novozym® 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. Biotechnol. Bioeng. 2008;99: 1518–1524. © 2007 Wiley Periodicals, Inc. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Biotechnology and Bioengineering 99 6 1518 1524 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
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 1‐octanol catalyzed by immobilized Candida antarctica lipase B (Novozym® 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. Biotechnol. Bioeng. 2008;99: 1518–1524. © 2007 Wiley Periodicals, Inc. |
format |
Article in Journal/Newspaper |
author |
Nordblad, Mathias Adlercreutz, Patrick |
spellingShingle |
Nordblad, Mathias Adlercreutz, Patrick Efficient enzymatic acrylation through transesterification at controlled water activity |
author_facet |
Nordblad, Mathias Adlercreutz, Patrick |
author_sort |
Nordblad, Mathias |
title |
Efficient enzymatic acrylation through transesterification at controlled water activity |
title_short |
Efficient enzymatic acrylation through transesterification at controlled water activity |
title_full |
Efficient enzymatic acrylation through transesterification at controlled water activity |
title_fullStr |
Efficient enzymatic acrylation through transesterification at controlled water activity |
title_full_unstemmed |
Efficient enzymatic acrylation through transesterification at controlled water activity |
title_sort |
efficient enzymatic acrylation through transesterification at controlled water activity |
publisher |
Wiley |
publishDate |
2007 |
url |
http://dx.doi.org/10.1002/bit.21706 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbit.21706 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.21706 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biotechnology and Bioengineering volume 99, issue 6, page 1518-1524 ISSN 0006-3592 1097-0290 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bit.21706 |
container_title |
Biotechnology and Bioengineering |
container_volume |
99 |
container_issue |
6 |
container_start_page |
1518 |
op_container_end_page |
1524 |
_version_ |
1800741397284782080 |