Reaction kinetics of immobilized αchymotrypsin in organic media 1. Influence at solvent polarity
Wehtje, Ernst LU ; Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1993)
In Biocatalysis and Biotransformation
7(3).
p.149-161
- Abstract
Esterification of N-acetyl phenylalanine with ethanol catalyzed by immobilized αchymotrypsin (EC 3.4.21.1) was studied in various reaction media. The effect of reaction medium polarity on enzymatic activity as well as equilibrium yield was measured. The reaction rate increased with increasing amounts of added water, reaching an optimum corresponding to water saturation of the reaction medium. Further additions of water resulted in decreased activity. Bell-shaped activity profiles were obtained for all reaction media tested. Reaction media consisting of pure solvents and of mixtures of solvents were used. The enzymatic activity and the equilibrium yield increased with decreased polarity of the medium. Maximum activity was found in a... (More)
Esterification of N-acetyl phenylalanine with ethanol catalyzed by immobilized αchymotrypsin (EC 3.4.21.1) was studied in various reaction media. The effect of reaction medium polarity on enzymatic activity as well as equilibrium yield was measured. The reaction rate increased with increasing amounts of added water, reaching an optimum corresponding to water saturation of the reaction medium. Further additions of water resulted in decreased activity. Bell-shaped activity profiles were obtained for all reaction media tested. Reaction media consisting of pure solvents and of mixtures of solvents were used. The enzymatic activity and the equilibrium yield increased with decreased polarity of the medium. Maximum activity was found in a reaction medium consisting of 80% diisopropyl ether and 20% heptane. The enzymatic activity obtained at optimal water additions in the different solvents and solvents mixtures could be correlated to the solubility of water and the log P of the medium. The equilibrium yield of the reaction was much more closely correlated to the solubility of water than the log P. Much lower enzymatic activity was obtained when solvent mixtures producing water-miscible media were created, than in mixtures producing water-immiscible media, such as mixtures of acetonitrile and diisopropyl ether. The equilibrium yield could be increased by decreasing the water content in the reaction medium, which reduced the water activity.
(Less)
- author
- Wehtje, Ernst
LU
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1993-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Equilibrium yields, Solvent mixtures, Solvent polarity, αchymotrypsin
- in
- Biocatalysis and Biotransformation
- volume
- 7
- issue
- 3
- pages
- 13 pages
- publisher
- Taylor & Francis
- external identifiers
-
- scopus:0011439158
- ISSN
- 1024-2422
- DOI
- 10.3109/10242429308997676
- language
- English
- LU publication?
- yes
- id
- 990609e6-aab5-4206-814a-27d45a6ce9d2
- date added to LUP
- 2019-06-22 09:22:36
- date last changed
- 2021-01-03 05:35:35
@article{990609e6-aab5-4206-814a-27d45a6ce9d2,
abstract = {{<p>Esterification of N-acetyl phenylalanine with ethanol catalyzed by immobilized αchymotrypsin (EC 3.4.21.1) was studied in various reaction media. The effect of reaction medium polarity on enzymatic activity as well as equilibrium yield was measured. The reaction rate increased with increasing amounts of added water, reaching an optimum corresponding to water saturation of the reaction medium. Further additions of water resulted in decreased activity. Bell-shaped activity profiles were obtained for all reaction media tested. Reaction media consisting of pure solvents and of mixtures of solvents were used. The enzymatic activity and the equilibrium yield increased with decreased polarity of the medium. Maximum activity was found in a reaction medium consisting of 80% diisopropyl ether and 20% heptane. The enzymatic activity obtained at optimal water additions in the different solvents and solvents mixtures could be correlated to the solubility of water and the log P of the medium. The equilibrium yield of the reaction was much more closely correlated to the solubility of water than the log P. Much lower enzymatic activity was obtained when solvent mixtures producing water-miscible media were created, than in mixtures producing water-immiscible media, such as mixtures of acetonitrile and diisopropyl ether. The equilibrium yield could be increased by decreasing the water content in the reaction medium, which reduced the water activity.</p>}},
author = {{Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{1024-2422}},
keywords = {{Equilibrium yields; Solvent mixtures; Solvent polarity; αchymotrypsin}},
language = {{eng}},
month = {{01}},
number = {{3}},
pages = {{149--161}},
publisher = {{Taylor & Francis}},
series = {{Biocatalysis and Biotransformation}},
title = {{Reaction kinetics of immobilized αchymotrypsin in organic media 1. Influence at solvent polarity}},
url = {{http://dx.doi.org/10.3109/10242429308997676}},
doi = {{10.3109/10242429308997676}},
volume = {{7}},
year = {{1993}},
}