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
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.