Effects of water activity on reaction rates and equilibrium positions in enzymatic esterifications
(1994) In Biotechnology and Bioengineering 44(5). p.549-556- Abstract
A technique of continuous water activity control was used to examine the effects of water activity on enzyme catalysis in organic media. Esterification catalyzed by Rhizopus arrhizus lipase was preferably carried out at a water activity of 0.33, which resulted in both maximal initial reaction rate and a high yield. When Pseudomonas lipase was used as catalyst it was beneficial to start the reaction at high water activity (giving the optimal reaction rate with this enzyme) and then shift to a lower water activity toward the end of the reaction to obtain a high yield. The apparent equilibrium constant of the reaction was influenced by the water activity of the organic solvent. © 1994 John Wiley & Sons, Inc.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8125c231-051a-471f-9d6c-940f2cf8dae4
- author
- Svensson, Ingemar LU ; Wehtje, Ernst LU ; Adlercreutz, Patrick LU and Mattiasson, Bo LU
- organization
- publishing date
- 1994-08-20
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- equilibrium constants, esterification, lipase, water activity control
- in
- Biotechnology and Bioengineering
- volume
- 44
- issue
- 5
- pages
- 8 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:0028486013
- ISSN
- 0006-3592
- DOI
- 10.1002/bit.260440502
- language
- English
- LU publication?
- yes
- id
- 8125c231-051a-471f-9d6c-940f2cf8dae4
- date added to LUP
- 2019-06-22 09:12:25
- date last changed
- 2021-05-16 05:49:08
@article{8125c231-051a-471f-9d6c-940f2cf8dae4, abstract = {{<p>A technique of continuous water activity control was used to examine the effects of water activity on enzyme catalysis in organic media. Esterification catalyzed by Rhizopus arrhizus lipase was preferably carried out at a water activity of 0.33, which resulted in both maximal initial reaction rate and a high yield. When Pseudomonas lipase was used as catalyst it was beneficial to start the reaction at high water activity (giving the optimal reaction rate with this enzyme) and then shift to a lower water activity toward the end of the reaction to obtain a high yield. The apparent equilibrium constant of the reaction was influenced by the water activity of the organic solvent. © 1994 John Wiley & Sons, Inc.</p>}}, author = {{Svensson, Ingemar and Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}}, issn = {{0006-3592}}, keywords = {{equilibrium constants; esterification; lipase; water activity control}}, language = {{eng}}, month = {{08}}, number = {{5}}, pages = {{549--556}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Biotechnology and Bioengineering}}, title = {{Effects of water activity on reaction rates and equilibrium positions in enzymatic esterifications}}, url = {{http://dx.doi.org/10.1002/bit.260440502}}, doi = {{10.1002/bit.260440502}}, volume = {{44}}, year = {{1994}}, }