Development of chia gum/alginate-polymer support for horseradish peroxidase immobilization and its application in phenolic removal

• Published in: Scientific reports Vol. 14; no. 1; p. 1362
• Main Authors: Mohamed, Saleh A., Elsayed, Alshaimaa M., Salah, Hala A., Barakat, Amal Z., Bassuiny, Roqaya I., Abdel-Mageed, Heidi M., Abdel-Aty, Azza M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 16.01.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 631/1647; 631/45; Affinity; Alginic acid; Biotechnology; Chlorophenol; Enzymes; Fourier transforms; Guaiacol; Heavy metals; High temperature; Horseradish peroxidase; Humanities and Social Sciences; Hydrogen peroxide; Immobilization; multidisciplinary; p-Chlorophenol; pH effects; Phenolic compounds; Phenols; Polymers; Salvia columbariae; Scanning electron microscopy; Science; Science (multidisciplinary); Thermal properties; Thermal stability; Urea
• DOI: 10.1038/s41598-024-51566-x
• ISSN: 2045-2322

Chia gum’s molecular structure with distinctive properties as well as the alginate-based hydrogel’s three-dimensionally cross-linked structure can provide a potent matrix for immobilization of enzyme. Herein, chia gum (CG)/alginate (A)-polymeric complex was synthesized and employed as a support material for the immobilization of horseradish peroxidase (HRP). HRP was successfully immobilized on the developed ACG-polymeric support, and the highest immobilization recovery (75%) was observed at 1.0% CG and 2% A, pH 7.0, and 50 units of the enzyme. The structure, morphology, and thermal properties of the prepared ACG-HRP were demonstrated using Fourier Transform Infrared (FTIR), Scanning Electron Microscope, and Thermogravimetric (TGA) analyses. ACG-HRP showed a good reusability (60%) over ten reuses. The immobilized ACG-HRP displayed an acidic pH optimum (6.0), a higher temperature optimum (50 °C), and improved thermal stability (30–50 °C) compared to the soluble HRP at pH 7.0, 40 °C and (30–40 °C), respectively. ACG-HRP has a lower affinity for hydrogen peroxide (H 2 O 2 ) and guaiacol and a higher oxidizing affinity for a number of phenolic substrates. The ACG-HRP demonstrated greater resistance to heavy metals, isopropanol, urea, Triton X-100, and urea, as well as improved efficiency for eliminating phenol and p -chlorophenol. The developed ACG-polymeric support provided improved enzyme properties, allowed the reuse of the immobilized HRP in 10 cycles, and made it promising for several biotechnological applications.