Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent
Academic Article
Publication Date:
2004
abstract:
Chloroperoxidase from Caldariomyces fumago catalyses the oxidation of 1,2-dihydronaphthalene to (1R,2R)-(+)-dihydroxytetrahydronaphthalene in homogenous citrate buffer/ionic liquid mixtures, using t-butyl hydroperoxide as 0) donor. It tolerates up to 30% (v/v) 1,3-dimethylimidazolium methylsulfate or 1-butyl-3-methylimidazolium methylsulfate. The enzyme activity in these ionic liquid co-solvent systems is retained for 24 h, but it falls to 3 h using non-ionic organic solvents such as t-BuOH or acetone.
Iris type:
01.01 Articolo in rivista
Keywords:
chloroperoxidase; enzyme stability; ionic liquid; stereoselectivity
List of contributors:
D'Antona, Nicola; Sanfilippo, Claudia; Nicolosi, Giovanni
Published in: