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Stability and stabilization of hydroxynitrile lyase in organic solvents

Costes, David LU ; Rotčenkovs, Gints ; Wehtje, Ernst LU and Adlercreutz, Patrick LU (2001) In Biocatalysis and Biotransformation 19(2). p.119-130
Abstract

The stability of hydroxynitrile lyase from Hevea brasiliensis has been studied in organic solvents. In dry solvents, the enzyme had half-lives in the range 1400-2500 hours. The enzyme half-life was one order of magnitude lower if the medium was water saturated. The substrates, aldehyde and hydrogen cyanide, were found to promote enzyme deactivation. The deactivation increased with substrate concentration, but was reduced in hydrophilic solvent. At high substrate concentration (2 M) in tert-butyl methyl ether, the enzyme half-life was 1.7 h when incubated with hydrogen cyanide while it was 1.0 h with 3-phenylpropionaldehyde. The addition of polyethylenimine, 125 mg per g of enzyme preparation, increased the enzyme half-life to 110 h when... (More)

The stability of hydroxynitrile lyase from Hevea brasiliensis has been studied in organic solvents. In dry solvents, the enzyme had half-lives in the range 1400-2500 hours. The enzyme half-life was one order of magnitude lower if the medium was water saturated. The substrates, aldehyde and hydrogen cyanide, were found to promote enzyme deactivation. The deactivation increased with substrate concentration, but was reduced in hydrophilic solvent. At high substrate concentration (2 M) in tert-butyl methyl ether, the enzyme half-life was 1.7 h when incubated with hydrogen cyanide while it was 1.0 h with 3-phenylpropionaldehyde. The addition of polyethylenimine, 125 mg per g of enzyme preparation, increased the enzyme half-life to 110 h when incubated with hydrogen cyanide and to 3.2 h with 3-phenylpropanaldehyde in tert-butyl methyl ether. Albumin and poly(ethylene glycol) gave similar stabilization effect.

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publishing date
type
Contribution to journal
publication status
published
subject
keywords
Hydroxynitrile lyase, Organic solvent, Polyethylenimine, Stability, Stabilization
in
Biocatalysis and Biotransformation
volume
19
issue
2
pages
12 pages
publisher
Taylor & Francis
external identifiers
  • scopus:0034918963
ISSN
1024-2422
DOI
10.3109/10242420109003640
language
English
LU publication?
yes
id
aea00315-23e3-44ae-a2c3-e9a7d69864c3
date added to LUP
2019-06-20 15:51:34
date last changed
2020-02-12 10:08:34
@article{aea00315-23e3-44ae-a2c3-e9a7d69864c3,
  abstract     = {<p>The stability of hydroxynitrile lyase from Hevea brasiliensis has been studied in organic solvents. In dry solvents, the enzyme had half-lives in the range 1400-2500 hours. The enzyme half-life was one order of magnitude lower if the medium was water saturated. The substrates, aldehyde and hydrogen cyanide, were found to promote enzyme deactivation. The deactivation increased with substrate concentration, but was reduced in hydrophilic solvent. At high substrate concentration (2 M) in tert-butyl methyl ether, the enzyme half-life was 1.7 h when incubated with hydrogen cyanide while it was 1.0 h with 3-phenylpropionaldehyde. The addition of polyethylenimine, 125 mg per g of enzyme preparation, increased the enzyme half-life to 110 h when incubated with hydrogen cyanide and to 3.2 h with 3-phenylpropanaldehyde in tert-butyl methyl ether. Albumin and poly(ethylene glycol) gave similar stabilization effect.</p>},
  author       = {Costes, David and Rotčenkovs, Gints and Wehtje, Ernst and Adlercreutz, Patrick},
  issn         = {1024-2422},
  language     = {eng},
  month        = {01},
  number       = {2},
  pages        = {119--130},
  publisher    = {Taylor & Francis},
  series       = {Biocatalysis and Biotransformation},
  title        = {Stability and stabilization of hydroxynitrile lyase in organic solvents},
  url          = {http://dx.doi.org/10.3109/10242420109003640},
  doi          = {10.3109/10242420109003640},
  volume       = {19},
  year         = {2001},
}