RESUMEN
D-hydantoinase from Vigna angularis was immobilized by covalent linkage to aminopropyl glass beads. Thermal stability, resistance to storage at different pH values and temperatures of this biocatalyst were studied. This enzyme preparation was used as a catalyst to prepare enantioenriched N-carbamoyl-D-phenylglycine, N-carbamyl-D-p-fluorophenylglycine and N-carbamoyl-D-p-trifluoromethylphenylglycine, using a stirred batch reactor. Reactions were conducted during eight repeated reaction cycles, without loss of enzymatic activity or variation of the enantiomeric excess of the respective product (>98%).
Asunto(s)
Amidohidrolasas/química , Enzimas Inmovilizadas , Glicina/química , Extractos Vegetales , Proteínas de Plantas/química , Plantas/enzimología , Reactores Biológicos , Catálisis , Estabilidad de Enzimas , Concentración de Iones de Hidrógeno , Modelos Moleculares , Estereoisomerismo , Temperatura , Factores de TiempoRESUMEN
D-Hydantoinase from Vigna angularis hydrolyzed rac-5-monosubstituted-hydantoins with polar and aromatic side chains and dihydrothymine but rac-5,5-disubstituted-hydantoins were not substrates of this enzyme. 5-Phenylhydantoin was the best substrate. By using this substrate, Ncarbamoyl-D-phenylglycine was obtained in quantitative yield and over 98% ee.