Lou_2005_Biotechnol.Lett_27_1387

Reference

Title : Hydroxynitrile lyase catalysis in ionic liquid-containing systems - Lou_2005_Biotechnol.Lett_27_1387
Author(s) : Lou WY , Xu R , Zong MH
Ref : Biotechnol Lett , 27 :1387 , 2005
Abstract :

The cleavage of mandelonitrile catalysed by hydroxynitrile lyases (HNL) from Prunus amygdalus (PaHNL) and Manihot esculenta (MeHNL) proceeded more rapidly in monophasic aqueous media containing 1-propyl-3-methylimidazolium tetrafluoroborate [C4MIm][BF4] than in media containing acetonitrile or THF. Both HNLs were much more thermostable in [C4MIm][BF4] than in acetonitrile or THF. The addition of each of the four ionic liquids 1-butyl-, 1-pentyl- and 1-hexyl-3-methylimidazolium tetrafluoroborates at 2-6% (v/v in the aqueous phase) increased both the enzyme activity and the product e.e. in the PaHNL-catalysed transcyanation in an aqueous/DIPE biphasic system. However, MeHNL was inactivated by the ionic liquids, as indicated by the decreased reaction rate, substrate conversion and product e.e.

PubMedSearch : Lou_2005_Biotechnol.Lett_27_1387
PubMedID: 16215854

Related information

Citations formats

Lou WY, Xu R, Zong MH (2005)
Hydroxynitrile lyase catalysis in ionic liquid-containing systems
Biotechnol Lett 27 :1387

Lou WY, Xu R, Zong MH (2005)
Biotechnol Lett 27 :1387