Interactions between enzymes and oxide colloidal particles and their influence on enzymatic activity

Produktbeschreibung

Enzyme immobilization on inorganic oxide particles is a widely employed technique that permits the reuse of costly enzymes in catalytic processes. The aim of this study was to investigate the effects of adsorption on ceramic particles on the catalytic activities of enzymes. The adsorption of the proteolytic enzyme α-chymotrypsin on silica, alumina, and titania was studied. The ­enzyme adsorption was specifically investigated by material characterization before and after adsorption, quantification of the adsorbed enzyme and detailed enzymatic activity measurements. Furthermore, the experimental results were interpreted based on complementary simulations. Covalent enzyme immobilization on amino-functionalized alumina and silica was also performed. Its effects on the enzymatic activity of α-chymotrypsin were additionally investigated by employing matrix-assisted laser desorption ionization time-of-flight mass spectroscopy.

Keywords: α-chymotrypsin, Adsorption, Colloidal particles, Physisorption, Covalent ­immobilization, Enzyme immobilization, Enzymatic activity, Alumina Silica Titania, α-chymotrypsin, Adsorption, Colloidal particles, Physisorption, Covalent ­immobilization, Enzyme immobilization, Enzymatic activity, Alumina Silica Titania