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

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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¡C in both batch stirred and fluidized-bed reactors.

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References

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Authors and Affiliations

  1. Dipartimento di Chimica, Ingegneria Chimica e Materiali, Universita di 'Aquila, Monteluco di Roio, 67040, L'Aquila, Italia

    F. Alfani, M. Cantarella, N. Cutarella & A. Gallifuoco

  2. Istituto G. Donegani, ENICHEM S.p.a., Via Fauser 4, 28100, Novara, Italia

    P. Golini & D. Bianchi

Authors
  1. F. Alfani
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  2. M. Cantarella
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  3. N. Cutarella
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  4. A. Gallifuoco
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  5. P. Golini
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  6. D. Bianchi
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Alfani, F., Cantarella, M., Cutarella, N. et al. Enzymatic conversion of cephalosporin C into glutaryl 7-aminocephalosporanic acid. A study in different reactor configurations. Biotechnology Letters 19, 175–178 (1997). https://doi.org/10.1023/A:1018324700707

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  • DOI: https://doi.org/10.1023/A:1018324700707

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