Conversion of cephalosporin C into glutaryl 7-aminocephalosporanic acid was catalysed by D-aminoacid oxidase from Trigonopsis variabilis, covalently immobilized on the polystyrenic resin Duolite A365. Spontaneous degradation of substrates was limited without depressing enzymatic activity at the optimum reaction pH 8.0. The highest product yield was 1.77 mmol per g of biocatalyst, attained at 15 degrees C in both batch stirred and fluidized-bed reactors.

Enzymatic conversion of cephalosporin C into glutaryl 7-aminocephalosporanic acid. A study in different reactor configurations

CANTARELLA M;GALLIFUOCO, ALBERTO;
1997-01-01

Abstract

Conversion of cephalosporin C into glutaryl 7-aminocephalosporanic acid was catalysed by D-aminoacid oxidase from Trigonopsis variabilis, covalently immobilized on the polystyrenic resin Duolite A365. Spontaneous degradation of substrates was limited without depressing enzymatic activity at the optimum reaction pH 8.0. The highest product yield was 1.77 mmol per g of biocatalyst, attained at 15 degrees C in both batch stirred and fluidized-bed reactors.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/20634
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