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

• Published in: Biotechnology, biotechnological equipment Vol. 37; no. 1; pp. 273 - 285
• Main Authors: Augustine, Maria, Madhusudhanan, Dhanya Thaikatt, Velayudhan, Mohanan Puzhavoorparambil
• Format: Journal Article
• Language: English
• Published: Sofia Taylor & Francis 17.02.2023; Taylor & Francis Ltd; Taylor & Francis Group
• Subjects: Adsorption; Amylases; Aniline; Chemistry; Core-shell structure; Deactivation; Enzymes; Formaldehyde; Heat inactivation; Immobilization; Inactivation; Investigations; Nanocomposite; Nanocomposites; Nanoparticles; Polyanilines; Process controls; Science; Storage stability; thermal deactivation; Thermal stability; α-Amylase
• ISSN: 1310-2818; 1314-3530
• DOI: 10.1080/13102818.2023.2182150

This study involves immobilizing α -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.