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Hydroxynitrile lyase-catalyzed synthesis of cyanohydrins in organic solvents Parameters influencing activity and enantiospecificity

Costes, David LU ; Wehtje, Ernst LU and Adlercreutz, Patrick LU (1999) In Enzyme and Microbial Technology 25(3-5). p.384-391
Abstract

(S)-Hydroxynitrile lyases from Hevea brasiliensis, Manihot esculenta, and Sorghum bicolor and (R)-hydroxynitrile lyase from Prunus amygdalus have been used as biocatalyst for the enantiospecific addition of hydrogen cyanide to aldehydes in organic solvents. The effects of the reaction parameters on the enzymatic reaction rate and product enantiomeric excess (e.e.) are presented. The reaction rate increased with the solvent hydrophobicity but highly hydrophobic solvents were not adapted to high hydrogen cyanide concentrations and provoked loss of activity and product e.e. In the synthesis of 3-phenylpropionaldehyde cyanohydrin catalyzed by (S)-hydroxynitrile lyases from H. brasiliensis, an e.e. value of 88 ± 1% was obtained under... (More)

(S)-Hydroxynitrile lyases from Hevea brasiliensis, Manihot esculenta, and Sorghum bicolor and (R)-hydroxynitrile lyase from Prunus amygdalus have been used as biocatalyst for the enantiospecific addition of hydrogen cyanide to aldehydes in organic solvents. The effects of the reaction parameters on the enzymatic reaction rate and product enantiomeric excess (e.e.) are presented. The reaction rate increased with the solvent hydrophobicity but highly hydrophobic solvents were not adapted to high hydrogen cyanide concentrations and provoked loss of activity and product e.e. In the synthesis of 3-phenylpropionaldehyde cyanohydrin catalyzed by (S)-hydroxynitrile lyases from H. brasiliensis, an e.e. value of 88 ± 1% was obtained under optimized reaction conditions. Lower enantiomeric excess values were obtained under conditions where the enzyme was inactivated: high hydrogen cyanide concentration, high solvent log P, low enzyme loading. At lower temperature (down to -5°C) the e.e. was increased for all four enzymes used. Enzymes from different sources used under identical optimized reaction conditions were found to yield cyanohydrins with very different enantiopurities. This intrinsic enantiospecificity is not an effect of spontaneous reactions independent of the enzyme. Copyright (C) 1999 Elsevier Science Inc.

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organization
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type
Contribution to journal
publication status
published
subject
keywords
Activity, Cyanohydrin, Enantiospecificity, Hydroxynitrile lyase, Organic solvent
in
Enzyme and Microbial Technology
volume
25
issue
3-5
pages
8 pages
publisher
Elsevier
external identifiers
  • scopus:0033180037
ISSN
0141-0229
DOI
10.1016/S0141-0229(99)00055-1
language
English
LU publication?
yes
id
7b950ffe-d826-4b53-b5ff-a4605c5c1c5d
date added to LUP
2019-06-20 16:01:37
date last changed
2020-02-12 10:08:34
@article{7b950ffe-d826-4b53-b5ff-a4605c5c1c5d,
  abstract     = {<p>(S)-Hydroxynitrile lyases from Hevea brasiliensis, Manihot esculenta, and Sorghum bicolor and (R)-hydroxynitrile lyase from Prunus amygdalus have been used as biocatalyst for the enantiospecific addition of hydrogen cyanide to aldehydes in organic solvents. The effects of the reaction parameters on the enzymatic reaction rate and product enantiomeric excess (e.e.) are presented. The reaction rate increased with the solvent hydrophobicity but highly hydrophobic solvents were not adapted to high hydrogen cyanide concentrations and provoked loss of activity and product e.e. In the synthesis of 3-phenylpropionaldehyde cyanohydrin catalyzed by (S)-hydroxynitrile lyases from H. brasiliensis, an e.e. value of 88 ± 1% was obtained under optimized reaction conditions. Lower enantiomeric excess values were obtained under conditions where the enzyme was inactivated: high hydrogen cyanide concentration, high solvent log P, low enzyme loading. At lower temperature (down to -5°C) the e.e. was increased for all four enzymes used. Enzymes from different sources used under identical optimized reaction conditions were found to yield cyanohydrins with very different enantiopurities. This intrinsic enantiospecificity is not an effect of spontaneous reactions independent of the enzyme. Copyright (C) 1999 Elsevier Science Inc.</p>},
  author       = {Costes, David and Wehtje, Ernst and Adlercreutz, Patrick},
  issn         = {0141-0229},
  language     = {eng},
  month        = {08},
  number       = {3-5},
  pages        = {384--391},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Hydroxynitrile lyase-catalyzed synthesis of cyanohydrins in organic solvents Parameters influencing activity and enantiospecificity},
  url          = {http://dx.doi.org/10.1016/S0141-0229(99)00055-1},
  doi          = {10.1016/S0141-0229(99)00055-1},
  volume       = {25},
  year         = {1999},
}