Biocatalyst engineering of Thermomyces Lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systems

Autor(es):Mostrar menos -

Silveira, Erick Abreu ^{[1, 2]} ; Moreno-Perez, Sonia ^[3] ; Basso, Alessandra ^[4] ; Serban, Simona ^[4] ; Pestana-Mamede, Rita ^[2] ; Tardioli, Paulo W. ^[1] ; Sanchez-Farinas, Cristiane ^[5] ; Castejon, Natalia ^[6] ; Fernandez-Lorente, Gloria ^[2] ; Rocha-Martin, Javier ^[2] ; Guisan, Jose M. ^[2]

Afiliação do(s) autor(es)

^[1] Univ Fed Sao Carlos, Sao Carlos, SP - Brazil

^[2] CSIC, ICP, Dept Biocatalysis, Campus UAM, Madrid 28049 - Spain

^[3] Univ Europea Madrid, Sch Biomed Sci, Pharm & Biotechnol Dept, Madrid - Spain

^[4] Purolite, Unit D, Llantrisant Business Pk, Llantrisant CF72 8LF, South Wales - Wales

^[5] Embrapa Instrumentat, Sao Carlos, SP - Brazil

^[6] Univ Autonoma Madrid, Fac Sci, Secc Dept Ciencias Alimentac, Hlth Lipids Grp, E-28049 Madrid - Spain

• Tipo de documento: Artigo Científico
• Fonte: Journal of Biotechnology; v. 289, p. 126-134, JAN 10 2019.
• Citações Web of Science: 2

Resumo

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 A of pore diameter) was 10-fold more active than TLL adsorbed on mesoporous supports (100-200 A 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 degrees C, fully preserving the activity after 20 days. In anhydrous oil at 40 degrees C, PEGylated TLL-Purolite C18 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. (AU)

• Processo FAPESP: 16/10636-8 - Da fábrica celular à biorrefinaria integrada Biodiesel-Bioetanol: uma abordagem sistêmica aplicada a problemas complexos em micro e macroescalas
• Beneficiário: Roberto de Campos Giordano
• Modalidade de apoio: Auxílio à Pesquisa - Programa BIOEN - Temático
• Processo FAPESP: 15/10530-2 - Aplicação de diferentes estratégias de engenharia enzimática para a obtenção de derivados imobilizados-estabilizados de novas lipases
• Beneficiário: Erick de Abreu Silveira
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Doutorado
• Processo FAPESP: 13/20826-0 - Produção de lipase pelo processo de fermentação combinada e sua aplicação na modificação de óleos e gorduras
• Beneficiário: Erick de Abreu Silveira
• Modalidade de apoio: Bolsas no Brasil - Doutorado