Catalytic Activity and Stability of Alkaline Phosphatase and β-Galactosidase on Aluminosilicate Adsorbents

Abstract This study investigates the catalytic activity and thermal stability of two enzymes—alkaline phosphatase and β-galactosidase—immobilized on the surface of BEA and MFI-type zeolites, as well as on natural aluminosilicate halloysite nanotubes (HNTs). The catalytic performance parameters (activity and Michaelis constant) were evaluated for all prepared catalysts. Thermal inactivation of the enzymes on the adsorbent surfaces was studied at 50, 55, and 60°C, and the first-order effective rate constants for inactivation (denaturation) and the corresponding activation energies were determined. The adsorbed enzyme layers partially retained their catalytic activity, while their thermal stability was significantly enhanced.