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Aspects of biocatalyst stability in organic solvents

Adlercreutz, Patrick LU orcid 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.

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author
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organization
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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}},
}