Thermal deactivation studies of alpha-amylase immobilized onto core-shell structured aniline formaldehyde crosslinked polyaniline magnetic nanocomposite

This study involves immobilizing alpha -amylase onto an aniline formaldehyde condensate cross-linked polyaniline magnetic nanocomposite (AFCCLPANIMg). To our knowledge, the utility of AFCCLPANIMg with a core-shell structure in enzyme immobilization has not received sufficient attention. The kinetic parameters were determined under optimal conditions, and the immobilized enzyme had a higher K-m value and a lower V-max value than the free enzyme, owing to the enzyme's conformational shift. The immobilized enzyme preserved 45% of its original activity after 12 cycles and 59% of its activity in 4-week storage stability testing. The thermal deactivation of the free and immobilized enzyme followed first-order kinetics. The D-values, t (1/2) and z value of the immobilized enzyme indicated better thermal stability than that of the free enzyme. The immobilized enzyme's high E-d value of 19.92 19.92 kJ mol(-1) defined its strong stability and resistance to heat inactivation.

Automated summary

This study focuses on immobilizing alpha-amylase onto a polyaniline magnetic nanocomposite with a core-shell structure. The immobilized enzyme showed different kinetic parameters compared to the free enzyme, indicating conformational changes. The immobilized enzyme demonstrated good stability and resistance to heat inactivation.