Covalent attachment of Candida rugosa lipase on chemically modified hybrid matrix of polysiloxane–polyvinyl alcohol with different activating compounds

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2008-02, Vol.61 (2), p.229-236
• Main Authors: Santos, Julio C., Mijone, Patrícia D., Nunes, Gisele F.M., Perez, Victor H., de Castro, Heizir F.
• Format: Article
• Language: English
• Subjects: 1-Butanol - metabolism; Butyric Acid - metabolism; Candida - drug effects; Candida - enzymology; Candida rugosa; Candida rugosa lipase; Chemical activation agents; Elements; Enzyme Activation - drug effects; Enzyme Activators - pharmacology; Enzyme immobilization; Enzyme Stability - drug effects; Enzymes, Immobilized - ultrastructure; Esterification - drug effects; Half-Life; Hydrogen-Ion Concentration; Hydrolysis - drug effects; Lipase - metabolism; Lipase - ultrastructure; Polysiloxane–polyvinyl alcohol matrix; Polyvinyl Alcohol - chemistry; Polyvinyl Alcohol - metabolism; Protein Denaturation - drug effects; Siloxanes - chemistry; Siloxanes - metabolism; Sol–gel technique; Spectroscopy, Fourier Transform Infrared; Temperature
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2007.08.006

Candida rugosa lipase was immobilized by covalent binding on hybrid matrix of polysiloxane–polyvinyl alcohol chemically modified with different activating agents as glutaraldehyde, sodium metaperiodate and carbonyldiimidazole. The experimental results suggested that functional activating agents render different interactions between enzyme and support, producing consequently alterations in the optimal reaction conditions. Properties of the immobilized systems were assessed and their performance on hydrolytic and synthetic reactions were evaluated and compared with the free enzyme. In hydrolytic reactions using p-nitrophenyl palmitate as substrate all immobilized systems showed higher thermal stability and optima pH and temperature values in relation to the free lipase. Among the activating compounds, carbonyldiimidazole resulted in a total recovery of activity on the support and the highest thermal stability. For the butyl butyrate synthesis, the best performance (molar conversion of 95% and volumetric productivity of 2.33 g L −1 h −1) was attained with the lipase immobilized on POS–PVA activated with sodium metaperiodate. The properties of the support and immobilized derivatives were also evaluated by scanning electron microscopy (SEM), energy dispersive X-ray spectroscopies and chemical composition (FTIR).