Abstract:
Fungal alpha amylase extracted from Aspergillus niger catalyses breakdown of starch into maltose. An enzyme with great industrial value used in food, pharmaceutical, brewing, and biofuel industries. Free a-amylase, nevertheless, is constrained by instability, low reusability, and troublesome recovery, limiting its practical application on an industrial scale. Immobilization of the enzyme on nanostructured materials provides an excellent approach to circumvent the disadvantages by enhancing enzyme stability, activity, and cost-effectiveness. The objective is to produce fungal aamylase, immobilize it on CuO/ZnO nanoparticles, and examine its kinetic, stability, and reusability properties in comparison to the free enzyme. CuO/ZnO hybrid nanoparticles were prepared by Northern catalpa leaf extract and used as a new support for immobilizing fungal a-amylase in this research. The nanoparticles and immobilized enzyme were characterized by FTIR, XRD, and SEM analysis. Free and immobilized a-amylase were compared in kinetic parameters, thermal and pH stability, reusability, and catalytic efficiency in cassava starch liquefaction. The immobilized a-amylase showed increased thermal stability, better catalytic activity and retained its activity after 10 cycles of reuse. The immobilized enzyme showed activity after 30 days of storage while free enzyme lost its activity after few days. These results make CuO/ZnO hybrid nanoparticles environmentally friendly, and biocompatible immobilization support for enzymes that provides sustainable and cost-effective solutions to starch processing and other industrial enzyme applications.
Page(s):
96-96
DOI:
DOI not available
Published:
Journal: 1st International Conference on "Recent Advances in Green Biotechnology and Climate Resilience", September 15-16, 2025, Volume: 1, Issue: 1, Year: 2025