Setembro 2018 vol. 1 num. 5 - XXII Congresso Brasileiro de Engenharia Química
Pôster - Open Access.
EFFECT OF ENZYME LOADING ON THE IMMOBILIZATION PARAMETERS OF A LIPASE ADSORBED ON FUNCTIONALIZED RICE HUSK SILICA
Commercial lipase from Thermomyces lanuginosus (TLL) was adsorbedon hydrophobic Octyl–SiO2 via interfacial activation and anion exchanger Amino–SiO2via ionic interaction. In this study, rice husk silica was used as matrix to prepare suchsupports. The effect of enzyme loading on the immobilization parameters has beenevaluated. Maximum immobilized protein loading of 12.3 and 21.9 mg/g for Amino–SiO2 and Octyl–SiO2 was observed, respectively. Experimental data on Octyl–SiO2 andAmino–SiO2 adsorption were well-fitted to Langmuir isotherm model. Similarhydrolytic activity values (between 630 and 645 IU/g of biocatalyst) were observed.However, strong diffusional limitation in hydrolysis reaction has been observed forimmobilized TLL on hydrophobic support (Octyl–SiO2). These results show the potentialapplication of the supports prepared in lipase immobilization for further use inbiotransformation reactions.
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MIGUEZ , J. P.; MACHADO, N. B. ; MENDES, A. A. ; "EFFECT OF ENZYME LOADING ON THE IMMOBILIZATION PARAMETERS OF A LIPASE ADSORBED ON FUNCTIONALIZED RICE HUSK SILICA", p. 1964-1968 . In: .
São Paulo: Blucher,
ISSN 2359-1757, DOI 10.5151/cobeq2018-PT.0520
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