Journal
BIOTECHNOLOGY & BIOTECHNOLOGICAL EQUIPMENT
Volume 37, Issue 1, Pages 273-285Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/13102818.2023.2182150
Keywords
Nanocomposite; alpha-amylase; immobilization; thermal stability; thermal deactivation
Categories
Ask authors/readers for more resources
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.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available