33468

IMMOBILIZATION OF MICROBIAL LIPASE BY PHYSICAL ADSORPTION ON HYDROPHOBIC SUPPORT AND APPLICATION IN 2-ETHYL-1-HEXYL OLEATE SYNTHESIS

Favoritar este trabalho

The aim of this work was to immobilize Thermomyces lanuginosus lipase (TLL) by physical adsorption on mesoporous poly-methacrylate particles (PMA) to catalyze alkyl esters synthesis by direct esterification of oleic acid and 2-ethyl-1-hexanol (biolubricant) in an organic medium. The catalytic properties of the biocatalysts prepared were assayed on the olive oil emulsion hydrolysis. The adsorption of TLL on PMA particles followed the Langmuir isotherm model (R2 = 0.9743). Maximum adsorption capacity was around 100 mg protein/g of support and hydrolytic activity around 650 IU/g was reached by offering 150 mg of protein/g of PMA partciles. The enzyme adsorption was a favorable process (free energy Gibbs varying from –17.0 to –7.4 kJ/mol). The biocatalyst prepared by offering 100 mg protein/g of support exhibited ester conversion percentage of 58% after 5 min of reaction under continuous agitation in an orbital shaker. PMA particles were found to be a suitable support for TLL immobilization, enabling the preparation of highly active biocatalysts in both aqueous and organic media.