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Inorganic nanometal complexes as enzyme carriers for enhanced stability and biocatalysts | ||
| Journal of University of Anbar for Pure Science | ||
| Volume 20, Issue 2, August 2026, Pages 252-263 PDF (408.98 K) | ||
| Document Type: Research Paper | ||
| DOI: 10.37652/juaps.2026.165452.1713 | ||
| Authors | ||
| Hanan Khamees Al-Dulymi* 1; Mustafa R AL-Shaheen2 | ||
| 1Department of Chemistry, College of Science, University of Anbar | ||
| 2Department of Biotechnology, College of Science, University of Anbar | ||
| Abstract | ||
| Immobilizing enzymes on nanostructured supports can greatly improve their stability and reusability. In the present study, nanostructured metal complexes of Zn, Cu, and Fe with various ligands were synthesized and applied as supports for lipase and glucose oxidase. The complexes, prepared by controlled precipitation, were characterized by XRD, FTIR, SEM, TEM, and TGA. Immobilization was evaluated using adsorption and covalent-binding methods. The results showed that the zinc citrate complex had the highest covalent immobilization efficiency of 92.3%. The immobilized enzymes had greater pH and temperature stability than the free enzymes, retaining approximately 90% of their initial activities at 60 °C, and could be used repeatedly. Kinetic studies revealed that the Km values and catalytic efficiencies of the immobilized enzymes decreased, with zinc citrate and ferric ethylenediamine imparting the highest stability to lipase and glucose oxidase, respectively. These findings emphasize the significance of inorganic nanometal complexes as versatile enzyme-stabilization platforms with extensive applications in green chemistry, pharmaceuticals, and bioenergy. | ||
| Keywords | ||
| Biocatalysts; Enzyme carriers; Inorganic nanometal; Stability | ||
| References | ||
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