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Formation of C—C bonds by mandelonitrile lyase in organic solvents

Wehtje, Ernst LU ; Adlercreutz, Patrick LU orcid and Mattiasson, Bo LU (1990) In Biotechnology and Bioengineering 36(1). p.39-46
Abstract

Mandelonitrile lyase (EC 4.1.2.10) catalyzes the formation of D‐mandelonitrile from HCN and benzaldehyde. Mandelonitrile lyase was immobilized by adsorption to support materials, for example, Celite. The enzyme preparations were used in diisopropyl ether for production of D‐mandelonitrile. In order to obtain optically pure D‐mandelonitrile it was necessary to use reaction conditions which favor the enzymatic reaction and suppress the competing spontaneous reaction, which yields a racemic mixture of D, L‐mandelonitrile. The effects of substrate concentrations, water content, and support materials on both the spontaneous and enzymatic reactions were studied. The enzymatic reaction was carried out under conditions where the importance of... (More)

Mandelonitrile lyase (EC 4.1.2.10) catalyzes the formation of D‐mandelonitrile from HCN and benzaldehyde. Mandelonitrile lyase was immobilized by adsorption to support materials, for example, Celite. The enzyme preparations were used in diisopropyl ether for production of D‐mandelonitrile. In order to obtain optically pure D‐mandelonitrile it was necessary to use reaction conditions which favor the enzymatic reaction and suppress the competing spontaneous reaction, which yields a racemic mixture of D, L‐mandelonitrile. The effects of substrate concentrations, water content, and support materials on both the spontaneous and enzymatic reactions were studied. The enzymatic reaction was carried out under conditions where the importance of the spontaneous reaction was negligible and high enantiomeric purity of D‐mandelonitrile was achieved (at least 98% enantiomeric excess). The operational stability of the enzyme preparations was studied in batch as well as in continuous systems. It was vital to control the water content in the system to maintain an active preparation. In a packed bed reactor the enzyme preparations were shown to be active and stable. The reactors were run for 50 h with only a small decrease in product yield.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology and Bioengineering
volume
36
issue
1
pages
8 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0025700661
ISSN
0006-3592
DOI
10.1002/bit.260360106
language
English
LU publication?
yes
id
cd5f1eca-8cb2-4361-a3f7-df437d69a90d
date added to LUP
2019-06-22 18:51:28
date last changed
2021-02-07 03:44:20
@article{cd5f1eca-8cb2-4361-a3f7-df437d69a90d,
  abstract     = {{<p>Mandelonitrile lyase (EC 4.1.2.10) catalyzes the formation of D‐mandelonitrile from HCN and benzaldehyde. Mandelonitrile lyase was immobilized by adsorption to support materials, for example, Celite. The enzyme preparations were used in diisopropyl ether for production of D‐mandelonitrile. In order to obtain optically pure D‐mandelonitrile it was necessary to use reaction conditions which favor the enzymatic reaction and suppress the competing spontaneous reaction, which yields a racemic mixture of D, L‐mandelonitrile. The effects of substrate concentrations, water content, and support materials on both the spontaneous and enzymatic reactions were studied. The enzymatic reaction was carried out under conditions where the importance of the spontaneous reaction was negligible and high enantiomeric purity of D‐mandelonitrile was achieved (at least 98% enantiomeric excess). The operational stability of the enzyme preparations was studied in batch as well as in continuous systems. It was vital to control the water content in the system to maintain an active preparation. In a packed bed reactor the enzyme preparations were shown to be active and stable. The reactors were run for 50 h with only a small decrease in product yield.</p>}},
  author       = {{Wehtje, Ernst and Adlercreutz, Patrick and Mattiasson, Bo}},
  issn         = {{0006-3592}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{1}},
  pages        = {{39--46}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Formation of C—C bonds by mandelonitrile lyase in organic solvents}},
  url          = {{http://dx.doi.org/10.1002/bit.260360106}},
  doi          = {{10.1002/bit.260360106}},
  volume       = {{36}},
  year         = {{1990}},
}