Lipase immobilization on smectite nanoclays: characterization and application to the epoxidation of alpha-pinene.

The immobilization of lipase B from Candida antarctica on smectite group nanoclays (Laponite, SWy-2 and Kunipia), as well as on their organically modified derivatives, was investigated. A combination of techniques, namely X-ray diffraction, thermal analysis, X-ray photoelectron and FT-IR spectroscopy, was used for characterization of the novel immobilized biocatalyst. Structural and biochemical characterization have revealed that the hydrophobic microenvironment created by the organo-modified clays induces minor changes on the secondary structure of the enzyme, resulting in enhanced catalytic behaviour in hydrophobic media.

Improving the catalytic performance of fungal laccases in monoterpene-based reaction systems.

Ternary systems consisting of monoterpenes (alpha-pinene or D-limonene), tert-butanol and water were used as reaction media to enhance the catalytic performance of laccases from various fungi sources (Trametes versicolor, T. hirsuta and Botrytis cinerea). The enzymes had improved catalytic efficiency (5- to 10-fold) in alpha-pinene-rich environment, while optimal reaction rates were in high-water content systems (15.