Biocatalyst Engineering of Thermomyces Lanuginosus Lipase Adsorbed on Hydrophobic Supports: Modulation of Enzyme Properties for Ethanolysis of Oil in Solvent-Free Systems

Publication date: Available online 19 November 2018Source: Journal of BiotechnologyAuthor(s): Erick Abreu Silveira, Sonia Moreno-Perez, Alessandra Basso, Simona Serban, Rita Pestana-Mamede, Paulo W. Tardioli, Cristiane Sanchez-Farinas, Natalia Castejon, Gloria Fernandez-Lorente, Javier Rocha-Martin, Jose M. GuisanAbstractDifferent immobilized biocatalysts of Thermomyces lanuginosus lipase (TLL) exhibited different properties for the ethanolysis of high oleic sunflower oil in solvent-free systems. TLL immobilized by interfacial adsorption on octadecyl (C-18) supports lost its 1,3-regioselectivity and produced more than 99% of ethyl esters. This reaction was influenced by mass-transfer limitations. TLL adsorbed on macroporous C-18 supports (616 Å of pore diameter) was 10-fold more active than TLL adsorbed on mesoporous supports (100-200 Å of pore diameter) in solvent-free systems. Both derivatives exhibited similar activity when working in hexane in the absence of diffusional limitations. In addition, TLL adsorbed on macroporous Purolite C-18 was 5-fold more stable than TLL adsorbed on mesoporous Sepabeads C-18. The stability of the best biocatalyst was 20-fold lower in anhydrous oil than in anhydrous hexane. Mild PEGylation of immobilized TLL greatly increased its stability in anhydrous hexane at 40 °C, fully preserving the activity after 20 days. In anhydrous oil at 40 °C, PEGylated TLL-Purolite C-18 retained 65% of its initial activity after six days compared to ...

Source: Journal of Biotechnology - November 21, 2018 Category: Biotechnology Source Type: research