Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber.

Summary

# Editorial Summary Horseradish peroxidase (HRP), an enzyme with applications in diagnostic assays and bioanalytical systems, was immobilized onto chemically modified polyester fiber to improve its practical utility and reusability in equine diagnostics and research applications. The researchers activated the fibre with glutaraldehyde before binding the enzyme, then systematically characterized both the immobilized and free enzyme across multiple parameters including pH optima, thermal performance, organic solvent tolerance, and long-term stability. Immobilized HRP retained robust activity across a broader temperature range (particularly between 50–60 °C) compared to its free counterpart, whilst operating optimally at pH 7 rather than the free enzyme's pH 8, with markedly superior storage stability that would extend shelf-life in field or laboratory settings. For equine professionals involved in point-of-care diagnostics or enzyme-based assay work, these findings suggest that immobilized enzyme systems could offer greater practical advantages in terms of durability and reduced degradation during storage and repeated use. This biotechnological approach potentially enables development of more robust, cost-effective diagnostic tools and stable enzyme reagents relevant to equine health screening and research protocols.

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Key Findings

• •Immobilized horseradish peroxidase on glutaraldehyde-activated poly(ethylene terephthalate) grafted acrylamide fiber achieved optimal activity at pH 7 compared to pH 8 for free enzyme
• •Immobilized HRP demonstrated higher relative activity at 50-60°C and superior storage stability compared to free HRP
• •Temperature profiles showed similar behavior between free and immobilized enzyme despite improved thermal performance of immobilized form in mid-range temperature zones