Cerium Oxide Nanoparticles‐Impregnated Alginate Surfaces for Covalent Immobilization of α‐Amylase via Glyoxal Activation: Stability and Kinetic Studies
Abstract
ABSTRACT Porcine pancreatic α‐amylase (E.C.3.2.1.1, 1,4‐α‐D‐glucan glucanohydrolase) was effectively immobilized on activated CeO 2 /Alginate nanocomposite via Schiff‐base covalent linkages using glyoxal. Characterization was performed using UV–vis, FTIR, XRD, TEM, FE‐SEM, and EDAX. Optimal conditions included coupling time (8 h), enzyme concentrations (1.2 mg/mL), and pH 7.5. Based on the outcomes, immobilized alpha‐amylases were found to be more thermally resistant than their free counterparts. These findings indicate that the CeO 2 /Alginate‐Gly‐α‐amylases bionanocomposite is a potential contender and versatile biocatalyst for large‐scale biotechnological and sustainable technologies.
Fields of Study & Subjects
Enzyme Catalysis and Immobilization
Enzyme Production and Characterization
Enzyme-mediated dye degradation
Publication details
- Journal / source
- Starch - Stärke
- Publisher
- Wiley
- Volume
- 78
- Issue
- 5
- Publication date
- 1 May 2026
- Language
- EN