Simona Butò

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D-amino acid oxidase from Trigonopsis variabilis was purified to homogeneity as a well resolved flavoprotein. Specific activity of pure enzyme was 86.6 U/mg at 30 degrees C and pH 8.5. Optimum pH for enzyme activity was 7.5 and optimum temperature was 55 degrees C. The enzyme is a non-glycosylated homodimer; the protein monomer had a M(r) of 38 +/- 2 kDa(More)
A process for the production (in a stirred tank reactor) of glutaryl-7-ACA from cephalosporin C using immobilized D-amino acid oxidase is described. Results so obtained under optimal conditions (1.2 mg coupled enzyme/L, pH 8.5, 2 mM cephalosporin C) point to a system which shows high conversion efficiency and a remarkable operational stability. No exogenous(More)
The study reports on the development of a bioreactor for the production of alpha-keto acids from D,L- or D-amino acids using Rhodotorula gracilis D-amino acid oxidase. D-amino acid oxidase was co-immobilized with catalase on Affi-Gel 10 matrix, and the reactor was operated as a continuous-stirred tank reactor (CSTR) or stirred tank with medium recycling(More)
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