Preparation of a biocatalyst via physical adsorption of lipase from Thermomyces lanuginosus on hydrophobic support to catalyze biolubricant synthesis by esterification reaction in a solvent-free system

[Display omitted] •Lipase from Thermomyces lanuginosus was immobilized on poly-methacrylate particles.•The biocatalysts were tested in isoamyl oleate (biolubricant) synthesis.•A satisfactory combination of high catalytic activity and reusability was reached.•Ester conversion ≈85% was reached after 3...

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Veröffentlicht in:Enzyme and microbial technology 2016-03, Vol.84, p.56-67
Hauptverfasser: Lage, Flávia A.P., Bassi, Jaquelinne J., Corradini, Maria C.C., Todero, Larissa M., Luiz, Jaine H.H., Mendes, Adriano A.
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Sprache:eng
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Zusammenfassung:[Display omitted] •Lipase from Thermomyces lanuginosus was immobilized on poly-methacrylate particles.•The biocatalysts were tested in isoamyl oleate (biolubricant) synthesis.•A satisfactory combination of high catalytic activity and reusability was reached.•Ester conversion ≈85% was reached after 30min of reaction in a solvent-free system.•The nature of the ester was characterized by spectroscopy analyses (ATR-FTIR and NMR). Lipase from Thermomyces lanuginosus (TLL) was immobilized on mesoporous hydrophobic poly-methacrylate (PMA) particles via physical adsorption (interfacial activation of the enzyme on the support). The influence of initial protein loading (5–200mg/g of support) on the catalytic properties of the biocatalysts was determined in the hydrolysis of olive oil emulsion and synthesis of isoamyl oleate (biolubricant) by esterification reaction. Maximum adsorbed protein loading and hydrolytic activity were respectively ≈100mg/g and ≈650 IU/g using protein loading of 150mg/g of support. The adsorption process followed the Langmuir isotherm model (R2=0.9743). Maximum ester conversion around 85% was reached after 30min of reaction under continuous agitation (200rpm) using 2500mM of each reactant in a solvent-free system, 45°C, 20%m/v of the biocatalyst prepared using 100mg of protein/g of support. Apparent thermodynamic parameters of the esterification reaction were also determined. Under optimal experimental conditions, reusability tests of the biocatalyst (TLL-PMA) after thirty successive cycles of reaction were performed. TLL-PMA fully retained its initial activity up to twenty two cycles of reaction, followed by a slight decrease around 8.6%. The nature of the product (isoamyl oleate) was confirmed by attenuated total reflection Fourier transform infrared (ATR-FTIR), proton (1H NMR) and carbon (13C NMR) nuclear magnetic resonance spectroscopy analyses.
ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2015.12.007