IMMOBILIZATION OF D-AMINO-ACID OXIDASE FROM DIFFERENT YEASTS - CHARACTERIZATION AND APPLICATION IN THE DEAMINATION OF CEPHALOSPORIN-C

Citation
P. Golini et al., IMMOBILIZATION OF D-AMINO-ACID OXIDASE FROM DIFFERENT YEASTS - CHARACTERIZATION AND APPLICATION IN THE DEAMINATION OF CEPHALOSPORIN-C, Enzyme and microbial technology, 17(4), 1995, pp. 324-329
Citations number
12
Categorie Soggetti
Biothechnology & Applied Migrobiology
ISSN journal
01410229
Volume
17
Issue
4
Year of publication
1995
Pages
324 - 329
Database
ISI
SICI code
0141-0229(1995)17:4<324:IODOFD>2.0.ZU;2-Q
Abstract
D-amino acid oxidase (DAAO)from Trigonopsis variabilis (CBS 4095) and Rhodotorula glutinis (NCIMB 40412) have been covalently linked to Duol ite A365, a polystyrenic support, functionalized with primary amino gr oups. The coupling to Duolite A365 was very effective for both enzymes , yielding an almost complete retention of the activity (>95%) in the case of the enzyme produced by T. variabilis. The immobilized D-amino acid oxidases exhibited a marked enhancement of stability against ther mal and pH inactivation. The optimization of the reaction conditions, as well as the long-term operational stability, were studied in the ca se of the deamination of cephalosporin C.