Increased enantioselectivity in the enzymatic hydrolysis of amino acid esters in the ionic liquid 1-butyl-3-methyl-imidazolium tetrafluoroborate

Abstract

The initial rate and enantioselectivity of enzymatic asymmetric hydrolysis of amino acid esters were examined in methylimidazolium-based ionic liquids with anions including tetrafluoroborate, chloride, bromide and bisulfate and in typical organic solvents. Papain displayed much higher enantioselectivity but lower activity in phosphate buffer solution of 1-butyl-3-methylimidazolium tetrafluoroborate BMIM·BF4 than in other media tested (i.e. E=100, V0=0.21 mM min−1 in BMIM·BF4, E=2, V0=0.43 mM min−1 in phosphate buffer, E=14–92, V0=0.22–0.25 mM min−1 in organic solvents for D,L-phenylglycine methyl ester). The influence of BMIM·BF4 on enzyme activity and enantioselectivity also varied with the substrate and the enzyme used. All of the enzymes assayed showed no activity or low enantioselectivity in the ILs with anions including chloride, bromide and bisulfate.