Immobilization of Trametes Versicolor Laccase onto Silica Aerogel via Covalent Attachment Method

Silica aerogels have a wide range of applications in enzyme immobilization studies as silica-based carrier materials with low density, high surface area and porosity. Their properties provide a more stable environment for enzymes and allow them to maintain their current activities. Immobilization of enzymes enables higher efficiency in enzyme-catalyzed industrial applications and reduces economic costs by reusing the immobilized enzyme. In this study, the enzyme laccase from T. versicolor was immobilized on aminated silica aerogel (SA-NH3 ) by covalent binding. SA-NH3 was prepared by a 24-hour aging process at 50 °C and had a surface area of 535 m²/g before amination. After amination, the surface area was calculated to be 43 m²/g at an APTES concentration of 1%. Analysis of the nitrogen adsorption/desorption isotherms showed that both SA and SA-NH3 had type IV isotherms and the material had a mesoporous structure. FTIR, XRF, SEM and zeta potential analyzes were performed for SA and SA-NH3 and it was confirmed that they had suitable characteristic properties for immobilization. The most suitable conditions for enzyme immobilization were a temperature of 25 °C, a pH of 4.5 and a glutaraldehyde concentration of 2%. Under these conditions, the immobilization efficiency was 35 % and the activity efficiency was 25%. This study showed that SA-NH3 is a potential carrier material for enzyme immobilization.