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

  • Estera Szwajcer Dey
  • Susanne Flygare
  • Klaus Mosbach


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.

Index Entries

Immobilizedd-amino acid oxidase production of glutaryl-7-ACA production of 7-ACA stabilization ofd-amino acid oxidase stabilization of cephalosporin C 



phenylmethylsulfonyl fluoride




D-amino acid oxidase


polyethylene glycol


controlled pore glass


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Copyright information

© Humana Press Inc. 1991

Authors and Affiliations

  • Estera Szwajcer Dey
    • 1
  • Susanne Flygare
    • 2
  • Klaus Mosbach
    • 2
  1. 1.Carlsberg Research LaboratoryGamle Carlsberg Vej 10ValbyDenmark
  2. 2.Department of Pure and Applied Biochemistry, Chemical CenterUniversity of LundLundSweden

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