Mineralization of Lipase from Thermomyces lanuginosus Immobilized on Methacrylate Beads Bearing Octadecyl Groups to Improve Enzyme Features

Lipase from Thermomyces lanuginosus (TLL) has been immobilized on Purolite Lifetech® ECR8806F (viz. methacrylate macroporous resin containing octadecyl groups, designated as C18-TLL), and the enzyme performance compared to that of octyl-agarose, agarose C8-TLL. The hydrolytic activity versus p-nitrophenol butyrate decreased significantly, a lower extent S-methyl mandelate (more than twofold), while triacetin R-methyl mandelate, was higher for biocatalyst prepared using C18 (up almost five-fold). Regarding stability, C18-TLL significantly more stable Next, biocatalysts were mineralized zinc, copper or cobalt phosphates. Mineralization increased this very S-isomer, effects C8-TLL diverse (hydrolytic increase decrease dependent metal substrate). zinc salt treatment stability both biocatalysts, but with impact agarose-C8-TLL. On contrary, treatments intensively C18-TLL. results show even enzymes following same strategy, differences in conformation cause mineralization have activity, specificity.