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Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis

AutorPereira Cipolatti, Eliane; Oliveira, Débora de; Pessela, Benevides C.
Palabras claveImmobilized enzymes
Enzyme biocatalysis
Enzyme activity
Fecha de publicación2016
CitaciónBiochemical Engineering Journal 112: 54-60 (2016)
ResumenThe adsorption of Thermomyces lanuginosus lipase (TLL) on PEGylated polyurethane particles as support permitted the development of several strategies to improve the properties of this commercial low-cost enzyme. The supports were synthesized by miniemulsion technique using isophoronediisocyanate (IPDI) and poly(ε-caprolactone) diol (PCL530) as monomers. The aqueous phase was composed of distilled water, surfactant sodium dodecyl sulfate (SDS), and poly(ethylene glycol) with different molar mass (PEG 400, 4000 or 6000). Polyethyleneimine (PEI) and trehalose were used to coat the PU-PEG polyurethane particles in order to increase the stability. In general, the coating with PEI (20%) allowed a greater stability of the derivatives. (100% of relative activity at 50 °C during 8 h). TLL immobilized on PEGylated polyurethane particles was efficiently used in the production of ethyl esters from fish oil compared to the free TLL (data not shown). The values of ethyl esters production of EPA and DHA were dependent on the support used for immobilization, which proved to be a determining factor in the activity. The highest selectivity obtained value was 45.8 for the PU-PEG4000-PEI20 derivative.
Identificadoresdoi: 10.1016/j.bej.2016.04.006
issn: 1369-703X
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