[Untitled]

Authors :: E. G. Oestreicher
O. A. C. Antunes
S. J. Sabino
M. B. Arcuri
Source :: Catalysis Letters. 79:17-19
Publication Year :: 2002
Publisher :: Springer Science and Business Media LLC, 2002.
Abstract: D-hydantoinase from Vigna angularis was covalently linked to aminopropyl glass beads. Comparative kinetic studies between immobilized and free D-hydantoinase showed that the immobilization procedure did not modify the catalytic properties nor the substrate specificity of the enzyme but increased its stability. In addition, N-carbamoyl-D-phenylglycine was produced in good yield with enantiomeric excess higher than 98%.