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Stabilization of D-amino acid oxidase from yeast trigonopsis variabilis used for production of glutaryl-7-aminocephalosporanic acid from cephalosporin C
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-aminocephalosporanic acid by D-amino acid oxidase (D-AAO), with the simultaneous production of equimolar amount of hydrogen peroxide, an...
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Published in: | Applied biochemistry and biotechnology 1991-03, Vol.27 (3), p.239-250 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | 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-aminocephalosporanic 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 as D-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 immobilized D-AAO on manganese oxide remained above 100% during the first 9 h of a semicontinuous conversion of cephalosporin C. |
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ISSN: | 0273-2289 1559-0291 |
DOI: | 10.1007/BF02921538 |