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

Ernst Wehtje, Patrick Adlercreutz, Bo Mattiasson

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish
Pages (from-to)39-46
Number of pages8
JournalBiotechnology and Bioengineering
Volume36
Issue number1
DOIs
Publication statusPublished - 1990 Jan 1

Subject classification (UKÄ)

  • Biocatalysis and Enzyme Technology

Fingerprint

Dive into the research topics of 'Formation of C—C bonds by mandelonitrile lyase in organic solvents'. Together they form a unique fingerprint.

Cite this