RESUMO
Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2-50% conversion in 3-16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.
Assuntos
Candida/enzimologia , Quitosana/química , Enzimas Imobilizadas/metabolismo , Proteínas Fúngicas/metabolismo , Lipase/metabolismo , Nanopartículas de Magnetita/química , Compostos de Vinila/química , Catálise , Enzimas Imobilizadas/química , Esterificação , Proteínas Fúngicas/química , Cinética , Lipase/química , EstereoisomerismoRESUMO
The Amano lipase from Pseudomonas fluorescens (L-AK) was covalently immobilized on various carbon nanomaterials (functionalized single-walled carbon nanotubes and graphene oxide) and tested for biodiesel production. Using the most active lipase preparation (covalently immobilized L-AK on SwCNTNH2 derivatized with glycerol diglycidyl ether) under optimal conditions, quasi-complete conversion (>99%) of sunflower oil was obtained after only 4 h reaction time. Moreover, the biocatalyst maintained more than 99% of its initial activity in the batch system after multiple recycling experiments.