Abstract
The new lipase formulation NS-40116 (Thermomyces lanuginosus) was immobilized in a hydrophobic matrix obtained by the sol-gel technique. Tetraethyl orthosilicate was used as the silica precursor. For the xerogel formation step, three catalysts were evaluated: acidic (HCl), basic (NH4OH), and nucleophilic (HBr). Polyethyleneglycol (PEG 1500) was used as a stabilizing agent (additive) and the influence of using it on the immobilization step was analyzed. The efficiency of the process was evaluated by measuring esterification activity. The basic xerogel with additive PEG was the immobilized formulation that presented the highest enzymatic activity, as well as greater yield (1,533%). The thermal stability in basic and acid immobilized with and without PEG showed the best results; even at 60°C, they exhibited approximately 50% of the initial activity and showed activity at 70°C. The free enzyme and the nucleophilic immobilized with and without PEG showed very reduced activity at 70°C, with a reduction of around 60% of the initial activity. The basic xerogel with PEG addition presented higher enzymatic activity, yield, number of cycles of use, and thermal stability than its free form and others xerogels, showing great potential for industrial applications.
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