Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent.
Claudia Sanfilippo, Nicola D'Antona, Giovanni Nicolosi
Index: Biotechnol. Lett. 26(23) , 1815-9, (2004)
Full Text: HTML
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 O2 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.
Related Compounds
Related Articles:
'Bridged' stilbene derivatives as selective cyclooxygenase-1 inhibitors.
2007-09-15
[Bioorg. Med. Chem. 15 , 6109-18, (2007)]
2007-06-14
[Chem. Commun. (Camb.) (22) , 2228-30, (2007)]
Asymmetric epoxidation using a singly-bound supported Katsuki-type (salen)Mn complex.
2002-04-21
[Chem. Commun. (Camb.) (8) , 886-7, (2002)]
Indatraline: synthesis and effect on the motor activity of Wistar rats.
2011-01-01
[Molecules 16(11) , 9421-38, (2011)]
Initial reactions in the oxidation of 1,2-dihydronaphthalene by Sphingomonas yanoikuyae strains.
1996-12-01
[Appl. Environ. Microbiol. 62(12) , 4388-94, (1996)]