American Chemical Society
la0c01594_si_001.pdf (1.74 MB)

Designing a Support for Lipase Immobilization Based On Magnetic, Hydrophobic, and Mesoporous Silica

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journal contribution
posted on 2020-08-20, 01:13 authored by Monique Deon, Natália Carminatti Ricardi, Rafaela Carvalho de Andrade, Plinho Francisco Hertz, Sabrina Nicolodi, Tania Maria Haas Costa, Roberta Bussamara, Edilson Valmir Benvenutti, Eliana Weber de Menezes
A mesoporous, magnetic, and hydrophobic material was designed step by step to act as a support for lipase immobilization. Its pore size (8.0 nm) is compatible with the size of lipase from Thermomyces lanuginosus (TLL), and its hydrophobic surface (contact angle of a water drop = 125°) was planned to interact with lipase on its interfacially activated form (open conformation). The presence of magnetite particles provides magnetic retrieval of the material and enables recyclability of the biocatalysts. Regarding immobilization parameters, the hydrophobic support was tested in comparison to the unmodified hydrophilic support in phosphate buffer solution (50 mmol L–1, pH 7.5) at 25 °C. Hydrophobicity was found to be critical for the amount of immobilized TLL (immobilization yield of 97% versus 36% for the hydrophilic support), whereas the hydrophilic support favors the native conformational state and substrate access to the enzyme’s catalytic site (specific activity of 5.7 versus 4.7 U g–1 for the hydrophobic support, even when it has higher TLL content). Therefore, the hydrophobic support immobilizes higher amounts of TLL and the hydrophilic support keeps the enzyme hyperactivated. Last, due to the stronger interactions of TLL with hydrophobic surfaces, the hydrophobic support offers better preservation of enzyme activity in repeated cycles (76% of activity retained after three cycles versus 50% for the hydrophilic support).