EFFECT OF ENZYME LOADING ON THE IMMOBILIZATION PARAMETERS OF A LIPASE ADSORBED ON FUNCTIONALIZED RICE HUSK SILICA

EFFECT OF ENZYME LOADING ON THE IMMOBILIZATION PARAMETERS OF A LIPASE ADSORBED ON FUNCTIONALIZED RICE HUSK SILICA

MIGUEZ , J. P.; MACHADO, N. B.; MENDES, A. A.

Pôster:

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.

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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DOI: 10.5151/cobeq2018-PT.0520

Referências bibliográficas

• [1] ADLERCREUTZ P, Immobilisation and application of lipases in organic media. Chem. Soc. Rev., v. 42, p. 6406-6436, 2013. ALVES MD, ARACRI FM, CREN EC, MENDES AA, Isotherm, kinetic, mechanism and thermodynamic studies of adsorption of a microbial lipase on a mesoporous and hydrophobic resin. Chem. Eng. J., v. 311, p. 1-12, 2017. BRADFORD MM, Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye. Anal. Biochem., v. 72, p. 248-254, 1976. VESCOVI V, KOPP W, GUISAN JM, GIORDANO RLC, MENDES AA, TARDIOLI PW, Improved catalytic properties of Candida antarctica lipase Bmulti-attached on tailor-made hydrophobic silica containing octyland multifunctional amino-glutaraldehyde spacer arms. Process Biochem., v. 51, p. 2055-2066, 2016. ZHANG S, GAO H, LI J, HUANG Y, ALSAEDI A, HAYAT T, XU X, WANG J, Rice husks as a sustainable silica source for hierarchical flower-like metal silicate architectures assembled into ultrathin nanosheets for adsorption and catalysis. J. Hazard. Mater., v. 321, p. 92-102, 2017.

Como citar:

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, 2018.
ISSN 23591757, DOI 10.5151/cobeq2018-PT.0520