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Journals / Hittite Journal of Science and Engineering / 2018 / Cilt: 5 - Sayı: 2

Enhanced Enzyme Activity with Ferritin Nanocages

Eylem TURAN
Pages
115–118
Publication Date
2022-10-18
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

This novel enzyme system displayed higher catalytic activity and enhanced stability

📌 3 Key Takeaways

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Objective & Hypothesis:I n this study, a novel enzyme system based on ferritin nanocages was designed. α-Amylase was covalently crosslinked on surface of ferritin nanocages by EDC/NHS.
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Key Findings & Data:The optimum temperature of immobilized enzyme shifted from 50 oC to 70 oC due to the ferritin nanocages.
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Conclusion & Impact:This novel enzyme system displayed higher catalytic activity and enhanced stability
🔬Design:Lab & Field Experiment
📍Scope:Comprehensive Sample
⚙️Variables:Ferritin nanocages · α-amylase · Enzyme immobilization

Abstract

I n this study, a novel enzyme system based on ferritin nanocages was designed. α-Amylase was covalently crosslinked on surface of ferritin nanocages by EDC/NHS. The activity of immobilized enzyme was monitored by using UV-vis spectrophotometer. The optimum temperature of immobilized enzyme shifted from 50 oC to 70 oC due to the ferritin nanocages. In addition, The Km and Vmax values of immobilized enzymes were 5.19 mg mL-1 and 3.3x10-5 U mg-1, respectively. This novel enzyme system displayed higher catalytic activity and enhanced stability

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Cite This Article

TURAN, E. (2022). Enhanced Enzyme Activity with Ferritin Nanocages. Hittite Journal of Science and Engineering, Cilt: 5 - Sayı: 2, 115–118. https://ajindex.com/articles/538050

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