A comparative study of covalent glucose oxidase and laccase immobilization techniques at powdered supports for biosensors fabrication
Abstrakt
In order to develop the optimal strategy and to deepen the knowledge in the field of enzyme immobilization, three different techniques of covalent binding for two enzymes (glucose oxidase and laccase) at powdered surfaces were compared. Immobilization protocol was optimized by changing supports (two mesoporous silica powders (SBA-15, MCM-41) and a cellulose powder), the functionalized groups introduced at support surfaces (-NH2 and -COOH), and the methods of activation (glutaraldehyde and carbodiimide).
Amino and carboxyl functionalized mesoporous silica and cellulose powders were prepared by silanization using (3-aminopropyl)triethoxysilane and carboxyethylsilanetriol, respectively. It was found that coupling of both enzymes by their -NH2 groups through glutaraldehyde to -NH2 functionalized supports, in particular SBA15-NH2 and cellulose-NH2 for glucose oxidase, MCM41-NH2 for laccase, showed the highest activity and the best stability.