Nicola D’Antona

Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent

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 O<>2<> 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.

Large scale preparation of enantiopure S-ketoprofen by biocatalysed kinetic resolution

Abstract Immobilised lipase from Candida antarctica (Novozym® 435) catalyses the enantioselective esterification of (±)-ketoprofen. The reaction conditions of the kinetic resolution have been investigated considering the kind of the solvent adopted and varying the nature of the alcohol. The use of methanol in dichloropropane allowes large scale separation, giving the desired S-ketoprofen with 96% ee as unreacted enantioform. The R-enantiomer, recovered as ester, easily undergoes chemical racemising hydrolysis and can be reused in the process.