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Effects of water activity on reaction rates and equilibrium positions in enzymatic esterifications

Svensson, Ingemar LU ; Wehtje, Ernst LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (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:
author
; ; and
organization
publishing date
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 &amp; 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}},
}