Immobilization of lipase from Candida rugosa onto niobium oxide. (November 2020)

• Record Type: Journal Article
• Authors: Mendonca Ferreira, Renata Deda; Brackmann, Rodrigo; Pereira, Ernandes Benedito; Costa da Rocha, Raquel Dalla
• Is Part Of: Biocatalysis and agricultural biotechnology. Number 30(2020)
• Publication Date: 2020-11
• Subjects: Lipase -- Adsorption -- Activity -- Niobic acid -- Support; Agricultural biotechnology -- Periodicals; Enzymes -- Biotechnology -- Periodicals; 660.6
• DOI: 10.1016/j.bcab.2020.101812
• Languages: English
• ISSNs: 1878-8181

Abstract

Abstract: Lipase from Candida rugosa (CRL) was immobilized via adsorption on niobium pentoxide. The best condition for adsorption was pH 6, 150 rpm and enzyme/support ratio of 8000 U gsupport −1 . The kinetic study resulted in a better fit for pseudo-first order kinetics, and Langmuir isotherm best fit the data. Adsorption thermodynamics showed that the adsorption was favorable, and it approached to physical adsorption. After immobilization process, the optimum pH and the affinity of the biocatalyst for the substrate decreased, and the optimum temperature increased. Niobium pentoxide immobilized derivative (IDNb) presented suitable thermal stability, preserving more than 50% of its residual activity after 60 min of incubation at 60 °C. After 60 days of storage at 4 °C, the recorded loss of activity for IDNb was 45%. Highlights: The effect of pH, agitation and enzyme/support ratio on adsorption process were evaluated. N2O5 was used in the adsorption of CRL with the best condition of pH6, 150 rpm and enzyme/support ratio of 8000 Ugsupport −1 . Kinetic, chemical equilibrium, and thermodynamic investigations were performed. The immobilized derivative preserved more than 50% of its residual activity after 60 days storage.