(175bc) Immobilization and kinetic studies of a microbial lipase from the fungal organism Candida rugosa on methacrylate polymer resins

Immobilization of a microbial lipase from the fungal organism Candida rugosa onto an epoxy-based resin (ECR8285) and an octadecyl-based polymer resin (ECR8806) (Purolite) was studied. Differential light scattering measurements suggested that surface adsorption of the lipase on the external polymer surface was the dominant mechanism for the immobilization. BET experiments showed that pore size increased with immobilization. Enzymatic tri-glyceride hydrolysis in a stirred reactor was used to compare performance of the immobilized enzyme with enzyme in free solution. Enhanced kinetics were observed for the immobilized enzymes compared with free enzyme. Temperature stability of the immobilized enzyme proved to be superior with optimum temperatures in the range of 50-53C. High retention of immobilized enzyme activity was observed in multicycle experiments. The surface modifiers, glutaraldehyde and 3-Aminopropyl triethoxysilane proved to have a negative effect on kinetics. Itaconic acid as modifier showed doubling of reaction rates compared to supports with no modifier.