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Activity and operational stability of immobilized mandelonitrile lyase in methanol/water mixtures

Wehtje, Ernst LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1988) In Applied Microbiology and Biotechnology 29(5). p.419-425
Abstract

The enzyme mandelonitrile lyase was covalently immobilized on solid support materials using different methods. Immobilization on porous silica using coupling with glutaraldehyde afforded preparations with high enzyme loading (up to 9% (w/w)). The immobilized enzyme was used in a packed bed reactor for the continuous production of d-mandelonitrile from benzaldehyde and cyanide. The influence of the flow rate, pH, substrate concentrations and enzyme loading on the reaction yield and the enantiomeric purity of the product was investigated. In order to suppress the competing spontaneous reaction, the enzymatic reaction must be rapid. A flow rate of 9.5 ml/min (0.1 M benzaldehyde and 0.3 M HCN) through a 3 ml reactor afforded a 86% yield of... (More)

The enzyme mandelonitrile lyase was covalently immobilized on solid support materials using different methods. Immobilization on porous silica using coupling with glutaraldehyde afforded preparations with high enzyme loading (up to 9% (w/w)). The immobilized enzyme was used in a packed bed reactor for the continuous production of d-mandelonitrile from benzaldehyde and cyanide. The influence of the flow rate, pH, substrate concentrations and enzyme loading on the reaction yield and the enantiomeric purity of the product was investigated. In order to suppress the competing spontaneous reaction, the enzymatic reaction must be rapid. A flow rate of 9.5 ml/min (0.1 M benzaldehyde and 0.3 M HCN) through a 3 ml reactor afforded a 86% yield of mandelonitrile with 92% enantiomeric excess. No leakage of enzyme occurred under continuous operation. One column was used continuously for 200 h without any decrease in yield or enantiomeric purity of the product. High concentrations of benzoic acid were shown to decrease the operational stability of the system.

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author
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publishing date
type
Contribution to journal
publication status
published
subject
in
Applied Microbiology and Biotechnology
volume
29
issue
5
pages
7 pages
publisher
Springer
external identifiers
  • scopus:0002952736
ISSN
0175-7598
DOI
10.1007/BF00269062
language
English
LU publication?
yes
id
d0edf94b-ef57-4de3-893d-285620941032
date added to LUP
2019-06-22 18:59:25
date last changed
2021-01-03 07:02:34
@article{d0edf94b-ef57-4de3-893d-285620941032,
  abstract     = {{<p>The enzyme mandelonitrile lyase was covalently immobilized on solid support materials using different methods. Immobilization on porous silica using coupling with glutaraldehyde afforded preparations with high enzyme loading (up to 9% (w/w)). The immobilized enzyme was used in a packed bed reactor for the continuous production of d-mandelonitrile from benzaldehyde and cyanide. The influence of the flow rate, pH, substrate concentrations and enzyme loading on the reaction yield and the enantiomeric purity of the product was investigated. In order to suppress the competing spontaneous reaction, the enzymatic reaction must be rapid. A flow rate of 9.5 ml/min (0.1 M benzaldehyde and 0.3 M HCN) through a 3 ml reactor afforded a 86% yield of mandelonitrile with 92% enantiomeric excess. No leakage of enzyme occurred under continuous operation. One column was used continuously for 200 h without any decrease in yield or enantiomeric purity of the product. High concentrations of benzoic acid were shown to decrease the operational stability of the system.</p>}},
  author       = {{Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0175-7598}},
  language     = {{eng}},
  month        = {{11}},
  number       = {{5}},
  pages        = {{419--425}},
  publisher    = {{Springer}},
  series       = {{Applied Microbiology and Biotechnology}},
  title        = {{Activity and operational stability of immobilized mandelonitrile lyase in methanol/water mixtures}},
  url          = {{http://dx.doi.org/10.1007/BF00269062}},
  doi          = {{10.1007/BF00269062}},
  volume       = {{29}},
  year         = {{1988}},
}