Biotechnology Letters 2004-12-01

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)

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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

  • dihydronaphthalene

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