Abreu Silveira, ErickMoreno-Pérez, SoniaBasso, AlessandraSerban, SimonaPestana-Mamede, RitaTardioli, PauloFarinas, CristianeCastejón, NataliaFernández-Lorente, GloriaRocha Martín, JavierGuisán, José2024-01-192024-01-192018Abreu Silveira, Erick, et al. «Biocatalyst Engineering of Thermomyces Lanuginosus Lipase Adsorbed on Hydrophobic Supports: Modulation of Enzyme Properties for Ethanolysis of Oil in Solvent-Free Systems». Journal of Biotechnology, vol. 289, enero de 2019, pp. 126-34. https://doi.org/10.1016/j.jbiotec.2018.11.014.0168-165610.1016/j.jbiotec.2018.11.014https://hdl.handle.net/20.500.14352/94108Funding Este trabajo contó con el apoyo del Ministerio de Economía, Industria y Competitividad de España (proyectos BIO2012-36861 y CTQ2015-70348). Javier Rocha-Martin agradece la beca Juan de la Cierva (número de subvención IJCI-2014-19260 ) financiada por el Ministerio de Economía, Industria y Competitividad de España . También agradecemos a la Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) por la concesión de la beca a Erick Abreu-Silveira y por las becas 2016/10636-8 , 2015/10530-2 y 2013/20826-0 .Different 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 10% of the activity retained by the unmodified biocatalyst. Macroporous and highly hydrophobic supports (e.g., Purolite C-18) seem to be very useful to prepare optimal immobilized biocatalysts for ethanolysis of oils by TLL in solvent-free systems.engBiocatalyst engineering of Thermomyces Lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systemsjournal articlehttps://doi.org/10.1016/j.jbiotec.2018.11.014restricted access577.1Ethyl oleateLipasesSolvent-free systemsHydrophobic adsorptionMacroporous supportsPEGylationBioquímica (Química)2302 Bioquímica