IMMOBILIZATION OF LIPASE FROM ENTEROBACTER AEROGENES E13 ON MODIFIED LIGNINS TO OBTAIN A NOVEL BIOCATALYST

Abstract

Lipase of Enterobacter aerogenes EI3 was immobilized by adsorption on lignins – wastes from lignocellulosic ethanol production. It was shown that the prehistory of the chosen lignins contributes to lipase immobilization: lignin obtained in the process of wood enzymatic hydrolysis for fuel ethanol production (SHF lignin) is a good solid support for lipase, which provides the highest activity yield and thermal stability (up to 50 °C) of immobilized lipase. Lipase immobilized on SHF lignin retained over 50 % of its original activity after 10 cycles of reuse. After three months of storage, immobilized lipase retained 80–97 % of its initial activity. The catalytic activity of the novel biocatalyst in the hydrolysis of triacylglycerols and the transesterification of biodiesel and rapeseed oil by octyl alcohol was close to that of the known commercial product Lipozyme RMIM.