A new generation of flowerlike horseradish peroxides as a nanobiocatalyst for superior enzymatic activity |
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Affiliation: | 1. Department of Analytical Chemistry, Faculty of Pharmacy, Erciyes University, 38039 Kayseri, Turkey;2. Nanotechnology Research Center, Erciyes University, Kayseri 38039, Turkey;1. Henan Provincial Key Laboratory of Surface and Interface Science, Zhengzhou University of Light Industry, Zhengzhou 450001, China;2. Henan Collaborative Innovation Centre of Environmental Pollution Control and Ecological Restoration, Zhengzhou University of Light Industry, Zhengzhou 450001, China;3. Chemistry and Chemical Engineering of Southeast University, Nanjing 211189, China;1. Henan Collaborative Innovation Center of Environmental Pollution Control and Ecological Resoration, Zhengzhou University of Light Industry, No. 166, Science Avenue, Zhengzhou 450001, PR China;2. State Laboratory of Surface and Interface Science of Henan Province, Zhengzhou University of Light Industry, No. 166, Science Avenue, Zhengzhou 450001, PR China;1. Department of Analytical Chemistry, Faculty of Pharmacy, Erciyes University, 38039 Kayseri, Turkey;2. Nanotechnology Research Center, Erciyes University, Kayseri, 38039 Turkey;3. Department of Chemistry, Faculty of Science, Erciyes University, Kayseri, 38039 Turkey |
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Abstract: | Although various supports including nanomaterials have been widely utilized as platforms for enzymes immobilization in order to enhance their catalytic activities, most of immobilized enzymes exhibited reduced activities compared to free enzymes. In this study, for the first time, we used iron ions (Fe2+) and horseradish peroxidase (HRP) enzyme together to synthesize flowerlike hybrid nanostructures with greatly enhanced activity and stability and reported an explanation of the enhancements in both catalytic activity and stability. We demonstrated that Fe2+-HRP hybrid nanoflower (HNF) showed catalytic activity of ∼512% and ∼710%, respectively when stored at +4 °C and room temperature (RT = 20 °C) compared to free HRP. In addition, the HNF stored at +4 °C lost only 2.9% of its original activity within 30 days while the HNF stored at RT lost approximately 10% of its original activity. However, under the same conditions, free HRP enzymes stored at +4 °C and RT lost 68% and 91% of their activities, respectively. We claim that the drastic increases in activities of HNF are associated with to high local HRP concentration in nanoscale dimension, appropriate HRP conformation, less mass transfer limitations, and role of Fe2+ ion as an activator for HRP. Further biosensors studies based on enhanced activity and stability of HNF are currently underway. |
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Keywords: | HRP Iron ion Catalytic activity Stability Hybrid nanoflower |
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