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Stabilization ofd-amino acid oxidase from yeastTrigonopsis variabilis used for production of glutaryl-7-aminocephalosporanic acid from cephalosporin C

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Abstract

The studies to improve the production of glutaryl-7-ACA from cephalosporin C are described in this paper.

During the conversion of cephalosporin C to keto-adipyl-7-aminocephalosporonic acid by d-amino acid oxidase (d-AAO), with the simultaneous production of equimolar amount of hydrogen peroxide, an incomplete nonenzymatic conversion of the keto form into the glutaryl form occurs, where cephalosporin C as well asd-AAO are partly destroyed in the presence of hydrogen peroxide.

d-AAO was immobilized to different carriers in order to achieve better enzyme stability. The activity of immobilizedd-AAO on manganese oxide remained above 100% during the first 9 h of a semicontinuous conversion of cephalosporin C. The presence of catalase coimmobilized with D-AAO and coupled to CNBr-activated Sepharose 4B improved the operation stability ofd-AAO.

An additional approach for the continuous transformation of cephalosporin C used whole cells ofTrigonopsis variabilis, containingd-AAO, immobilized to magnetic iron oxide particles.

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Abbreviations

PMSF:

phenylmethylsulfonyl fluoride

2,4-DNPH:

2,4-dinitrophenylhydrazine

D-AAO:

D-amino acid oxidase

PEG:

polyethylene glycol

CPG:

controlled pore glass

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Authors and Affiliations

  1. Carlsberg Research Laboratory, Gamle Carlsberg Vej 10, DK-2500, Valby, Copenhagen, Denmark

    Estera Szwajcer Dey

  2. Department of Pure and Applied Biochemistry, Chemical Center, University of Lund, PO Box 124, S-221 00, Lund, Sweden

    Susanne Flygare & Klaus Mosbach

Authors
  1. Estera Szwajcer Dey
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  2. Susanne Flygare
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  3. Klaus Mosbach
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Dey, E.S., Flygare, S. & Mosbach, K. Stabilization ofd-amino acid oxidase from yeastTrigonopsis variabilis used for production of glutaryl-7-aminocephalosporanic acid from cephalosporin C. Appl Biochem Biotechnol 27, 239–250 (1991). https://doi.org/10.1007/BF02921538

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  • DOI: https://doi.org/10.1007/BF02921538

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