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.
(Less)
- author
- Costes, David
LU
; Wehtje, Ernst
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 2001-01-22
- 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
- 2025-10-14 13:05:00
@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}},
keywords = {{Activity; Cross-linking; Crystal; Hydroxynitrile lyase; Stability}},
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}},
}