Hydroxynitrile lyase catalysis in ionic liquid-containing systems.
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.
Lou
Wen-Yong
WY
Department of Biotechnology, South China University of Technology, 510640, Guangzhou, P.R. China.
Xu
Ruo
R
Zong
Min-Hua
MH
D000097:Acetonitriles / Q000737:chemistry* / Q000378:metabolism; D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000378:metabolism; D001881:Borates / Q000737:chemistry; D002384:Catalysis; D004795:Enzyme Stability; D006856:Hydrogen Cyanide / Q000737:chemistry / Q000378:metabolism; D007093:Imidazoles / Q000737:chemistry; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D002365:Manihot / Q000201:enzymology; D008956:Models, Chemical; D009570:Nitriles / Q000737:chemistry / Q000378:metabolism; D027861:Prunus / Q000201:enzymology; D012997:Solvents / Q000737:chemistry; D013379:Substrate Specificity
D000097:Acetonitriles; D001881:Borates; D007093:Imidazoles; D007477:Ions; D009570:Nitriles; D012997:Solvents; D006856:Hydrogen Cyanide; C045516:mandelonitrile; C010833:acetone cyanohydrin; D000446:Aldehyde-Lyases; C079359:hydroxymandelonitrile lyase