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<p>This study explores the green synthesis of an alginate–cobalt ferrite (Alg–CoFe<sub>2</sub>O<sub>4</sub>) composite using <i>Brachychiton populneus</i> extract for horseradish peroxidase (HRP) immobilization, targeting enhanced enzyme stability and reusability. The Alg–CoFe<sub>2</sub>O<sub>4</sub> composite, synthesized via co-precipitation and calcination at 600&#xa0;°C, was characterized using XRD, VSM, SEM–EDX, BET, FT-IR, and zeta potential analysis, confirming its structural, magnetic, and surface properties. HRP immobilization via glutaraldehyde crosslinking achieved a high immobilization yield of 84%, attributed to the composite’s high surface area and covalent binding efficiency. Kinetic analysis revealed an increased Km (30&#xa0;mM) and Vmax (5.88&#xa0;µmol/min) for HRP@Alg–CoFe<sub>2</sub>O<sub>4</sub>, indicating enhanced catalytic efficiency with reduced substrate affinity. The immobilized enzyme exhibited superior tolerance to organic solvents, retaining 149% activity in n-hexane. In addition, it retained 71% activity after 10 cycles and 74% after 8&#xa0;weeks of storage at 4&#xa0;°C, outperforming free HRP. Optimal conditions shifted from pH 6.5 to 7.0 and from 50 to 60&#xa0;°C, reflecting improved environmental resilience. This study highlights HRP@Alg–CoFe<sub>2</sub>O<sub>4</sub> as a robust biocatalyst, offering promising applications in wastewater treatment and industrial bioprocesses.</p>

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Sustainable synthesis of alginate–cobalt ferrite nanocomposites for horseradish peroxidase immobilization: enhanced stability, reusability, and catalytic efficiency

  • 期刊论文

  • 发表日期：

    2025年4月23日

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  • Abdullah N. Alotaibi,
  • Abdullah Al-Dakhil,
  • Hayam A. Alwabsi,
  • Ibrahim O. Althobaiti,
  • Reda M. El-Shishtawy,
  • Yaaser Q. Almulaiky

摘要

This study explores the green synthesis of an alginate–cobalt ferrite (Alg–CoFe2O4) composite using Brachychiton populneus extract for horseradish peroxidase (HRP) immobilization, targeting enhanced enzyme stability and reusability. The Alg–CoFe2O4 composite, synthesized via co-precipitation and calcination at 600 °C, was characterized using XRD, VSM, SEM–EDX, BET, FT-IR, and zeta potential analysis, confirming its structural, magnetic, and surface properties. HRP immobilization via glutaraldehyde crosslinking achieved a high immobilization yield of 84%, attributed to the composite’s high surface area and covalent binding efficiency. Kinetic analysis revealed an increased Km (30 mM) and Vmax (5.88 µmol/min) for HRP@Alg–CoFe2O4, indicating enhanced catalytic efficiency with reduced substrate affinity. The immobilized enzyme exhibited superior tolerance to organic solvents, retaining 149% activity in n-hexane. In addition, it retained 71% activity after 10 cycles and 74% after 8 weeks of storage at 4 °C, outperforming free HRP. Optimal conditions shifted from pH 6.5 to 7.0 and from 50 to 60 °C, reflecting improved environmental resilience. This study highlights HRP@Alg–CoFe2O4 as a robust biocatalyst, offering promising applications in wastewater treatment and industrial bioprocesses.