Aspects of biocatalyst stability in organic solvents
Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1987)
In Biocatalysis and Biotransformation
1(2).
p.99-108
- Abstract
The stability of biocatalysis in systems containing organic solvents is reviewed. Among the examples presented are homogeneous mixtures of water and water-miscible organic solvents, aqueous/organic two-phase systems, solid biocatalysts suspended in organic solvents, enzymes in reverse micelles and modified enzymes soluble in water immiscible solvents. The stability of biocatalysts in organic solvents depends very much on the conditions. The hydrophobicity or the polarity of the solvent is clearly of great importance. More hydrophobic solvents (higher log P values) are less harmful to enzymes than less hydrophobic solvents. The water content of the system is a very important parameter. Some water is essential for enzymatic activity;... (More)
The stability of biocatalysis in systems containing organic solvents is reviewed. Among the examples presented are homogeneous mixtures of water and water-miscible organic solvents, aqueous/organic two-phase systems, solid biocatalysts suspended in organic solvents, enzymes in reverse micelles and modified enzymes soluble in water immiscible solvents. The stability of biocatalysts in organic solvents depends very much on the conditions. The hydrophobicity or the polarity of the solvent is clearly of great importance. More hydrophobic solvents (higher log P values) are less harmful to enzymes than less hydrophobic solvents. The water content of the system is a very important parameter. Some water is essential for enzymatic activity; however, the stability of enzymes decreases with increasing water content. Mechanisms of enzyme inactivation are discussed.
(Less)
- author
- Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1987-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Biocatalyst stability, Biocatalysts in organic solvents, Bioorganic synthesis, Enzyme stability, Enzymes in organic solvents
- in
- Biocatalysis and Biotransformation
- volume
- 1
- issue
- 2
- pages
- 10 pages
- publisher
- Taylor & Francis
- external identifiers
-
- scopus:0002889301
- ISSN
- 1024-2422
- DOI
- 10.3109/10242428709040134
- language
- English
- LU publication?
- yes
- id
- bbebfb2b-8555-4257-a997-e11306f7ed70
- date added to LUP
- 2019-06-22 19:10:24
- date last changed
- 2022-02-18 02:24:29
@article{bbebfb2b-8555-4257-a997-e11306f7ed70,
abstract = {{<p>The stability of biocatalysis in systems containing organic solvents is reviewed. Among the examples presented are homogeneous mixtures of water and water-miscible organic solvents, aqueous/organic two-phase systems, solid biocatalysts suspended in organic solvents, enzymes in reverse micelles and modified enzymes soluble in water immiscible solvents. The stability of biocatalysts in organic solvents depends very much on the conditions. The hydrophobicity or the polarity of the solvent is clearly of great importance. More hydrophobic solvents (higher log P values) are less harmful to enzymes than less hydrophobic solvents. The water content of the system is a very important parameter. Some water is essential for enzymatic activity; however, the stability of enzymes decreases with increasing water content. Mechanisms of enzyme inactivation are discussed.</p>}},
author = {{Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{1024-2422}},
keywords = {{Biocatalyst stability; Biocatalysts in organic solvents; Bioorganic synthesis; Enzyme stability; Enzymes in organic solvents}},
language = {{eng}},
month = {{01}},
number = {{2}},
pages = {{99--108}},
publisher = {{Taylor & Francis}},
series = {{Biocatalysis and Biotransformation}},
title = {{Aspects of biocatalyst stability in organic solvents}},
url = {{http://dx.doi.org/10.3109/10242428709040134}},
doi = {{10.3109/10242428709040134}},
volume = {{1}},
year = {{1987}},
}