Stability of immobilized D-hydantoinase from Vigna angularis and repeated cycles of highly enantioenriched production of N-carbamoyl-D-phenylglycines.
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%).
Arcuri
M B
MB
Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brasil.
Antunes
O A C
OA
Machado
S P
SP
Almeida
C H F
CH
Oestreicher
E G
EG
D000581:Amidohydrolases / Q000737:chemistry*; D019149:Bioreactors; D002384:Catalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D005998:Glycine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D010936:Plant Extracts; D010940:Plant Proteins / Q000737:chemistry*; D010944:Plants / Q000201:enzymology*; D013237:Stereoisomerism; D013696:Temperature; D013997:Time Factors
D004800:Enzymes, Immobilized; D010936:Plant Extracts; D010940:Plant Proteins; D000581:Amidohydrolases; C020047:dihydropyrimidinase; D005998:Glycine