Abstract:
Lipase from Candida antarctica A was immobilized for the first time by sol-gel entrapment. Two immobilization methods, with binary and ternary silane precursor mixtures containing tetramethoxysilane and trimethoxysilanes with alkyl or aryl groups and an ionic liquid as additive, have been applied. The catalytic activity and enantioselectivity of the immobilized biocatalysts were evaluated in the transacylation of aliphatic sec-alcohols with vinyl acetate. Depending on the sol-gel entrapment method applied, we obtained biocatalysts with excellent transesterification activity (> 0.705 μmole•h-1•mg-1) or with high enantiomeric ratio
(E >110) for the tested substrates. These results demonstrate the high biocatalytic potential of Candida antarctica A lipase and open new perspectives in future applications.
Keywords:
Candida antarctica A lipase, sol-gel entrapment, acylation, enantioselectivity
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