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Cross-linked crystals of hydroxynitrile lyase as catalyst for the synthesis of optically active cyanohydrins

Costes, David LU ; Wehtje, Ernst LU and Adlercreutz, Patrick LU (2001) In Journal of Molecular Catalysis - B Enzymatic 11(4-6). p.607-612
Abstract

Purified hydroxynitrile lyase (HNL) from Manihot esculenta was crystallized by the sitting-drop vapour-diffusion method. The bipyramidal crystals formed (10-20 μm) were cross-linked with different amounts of glutaraldehyde and used as biocatalyst for the synthesis of optically active cyanohydrins. The cross-linked crystals were more stable than Celite-immobilized enzymes when incubated in organic solvents, especially in polar solvents. After six consecutive batch reactions in dibutylether, the remaining activity of the cross-linked crystals was more than 70 times higher than for the immobilized enzymes. Nevertheless, the specific activity of the cross-linked crystals (per milligram protein) was reduced compared to the activity of... (More)

Purified hydroxynitrile lyase (HNL) from Manihot esculenta was crystallized by the sitting-drop vapour-diffusion method. The bipyramidal crystals formed (10-20 μm) were cross-linked with different amounts of glutaraldehyde and used as biocatalyst for the synthesis of optically active cyanohydrins. The cross-linked crystals were more stable than Celite-immobilized enzymes when incubated in organic solvents, especially in polar solvents. After six consecutive batch reactions in dibutylether, the remaining activity of the cross-linked crystals was more than 70 times higher than for the immobilized enzymes. Nevertheless, the specific activity of the cross-linked crystals (per milligram protein) was reduced compared to the activity of immobilized enzymes. The product enantiopurity was independent of the type of enzyme preparation used.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Activity, Cross-linking, Crystal, Hydroxynitrile lyase, Stability
in
Journal of Molecular Catalysis - B Enzymatic
volume
11
issue
4-6
pages
6 pages
publisher
Elsevier
external identifiers
  • scopus:0035931533
ISSN
1381-1177
DOI
10.1016/S1381-1177(00)00057-6
language
English
LU publication?
yes
id
489d3b1c-bd3b-46d2-a3ae-bba8c6345798
date added to LUP
2019-06-20 15:45:35
date last changed
2020-01-13 02:04:14
@article{489d3b1c-bd3b-46d2-a3ae-bba8c6345798,
  abstract     = {<p>Purified hydroxynitrile lyase (HNL) from Manihot esculenta was crystallized by the sitting-drop vapour-diffusion method. The bipyramidal crystals formed (10-20 μm) were cross-linked with different amounts of glutaraldehyde and used as biocatalyst for the synthesis of optically active cyanohydrins. The cross-linked crystals were more stable than Celite-immobilized enzymes when incubated in organic solvents, especially in polar solvents. After six consecutive batch reactions in dibutylether, the remaining activity of the cross-linked crystals was more than 70 times higher than for the immobilized enzymes. Nevertheless, the specific activity of the cross-linked crystals (per milligram protein) was reduced compared to the activity of immobilized enzymes. The product enantiopurity was independent of the type of enzyme preparation used.</p>},
  author       = {Costes, David and Wehtje, Ernst and Adlercreutz, Patrick},
  issn         = {1381-1177},
  language     = {eng},
  month        = {01},
  number       = {4-6},
  pages        = {607--612},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Catalysis - B Enzymatic},
  title        = {Cross-linked crystals of hydroxynitrile lyase as catalyst for the synthesis of optically active cyanohydrins},
  url          = {http://dx.doi.org/10.1016/S1381-1177(00)00057-6},
  doi          = {10.1016/S1381-1177(00)00057-6},
  volume       = {11},
  year         = {2001},
}