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%.
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