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

Key Points

• This research aims to evaluate the catalytic activity and thermal stability of alkaline phosphatase and β-galactosidase immobilized on various adsorbents.
• Immobilization of enzymes on BEA and MFI-type zeolites and halloysite nanotubes (HNTs)
• Evaluation of catalytic performance parameters including activity and Michaelis constant
• Study of thermal inactivation at temperatures of 50°C, 55°C, and 60°C
• Determination of first-order effective rate constants for inactivation and activation energies
• Enzymes retained partial catalytic activity when immobilized
• Thermal stability of enzymes was significantly enhanced on the adsorbent surfaces
• Determined activation energy values indicate improved enzyme performance at elevated temperatures

Abstract