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Insight into Bioactivity of In-situ Trapped Enzyme-Covalent-Organic Frameworks |
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| Authors: | Dr Jieying Liang Dr Juanfang Ruan Dr Bosiljka Njegic Dr Aditya Rawal Prof Jason Scott Prof Jiangtao Xu Prof Cyrille Boyer Prof Kang Liang |
| Institution: | 1. School of Chemical Engineering and Australian Centre for NanoMedicine, The University of New South Wales, Sydney, NSW 2052 Australia;2. Electron Microscope Unit, Mark Wainwright Analytical Centre, The, University of New South Wales, Sydney, NSW 2052 Australia;3. Nuclear Magnetic Resonance Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052 Australia
Contribution: Formal analysis (supporting), Methodology (supporting);4. Nuclear Magnetic Resonance Facility, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052 Australia Contribution: Data curation (supporting), Methodology (supporting);5. School of Chemical Engineering and Australian Centre for NanoMedicine, The University of New South Wales, Sydney, NSW 2052 Australia Contribution: Data curation (supporting);6. School of Chemical Engineering and Australian Centre for NanoMedicine, The University of New South Wales, Sydney, NSW 2052 Australia Contribution: Methodology (supporting) |
| Abstract: | Selecting a suitable support material for enzyme immobilization with excellent biocatalytic activity and stability is a critical aspect in the development of functional biosystems. The highly stable and metal-free properties of covalent-organic frameworks (COFs) make them ideal supports for enzyme immobilization. Herein, we constructed three kinds of COFs via a biofriendly and one-pot synthetic strategy at room temperature in aqueous solution. Among the three developed COFs (COF-LZU1, RT-COF-1 and ACOF-1), the horseradish peroxidase (HRP)-incorporated COF-LZU1 is found to retain the highest activity. Structural analysis reveals that a weakest interaction between the hydrated enzyme and COF-LZU1, an easiest accessibility by the COF-LZU1 to the substrate, as well as an optimal conformation of enzyme together promote the bioactivity of HRP-COF-LZU1. Furthermore, the COF-LZU1 is revealed to be a versatile nanoplatform for encapsulating multiple enzymes. The COF-LZU1 also offers superior protection for the immobilized enzymes under harsh conditions and during recycling. The comprehensive understanding of interfacial interactions of COF host and enzyme guest, the substrate diffusion, as well as the enzyme conformation alteration within COF matrices represents an opportunity to design the ideal biocatalysts and opens a broad range of applications of these nanosystems. |
| Keywords: | Bioactivity Biocatalysis Covalent-Organic Frameworks Enzymes Porous Microreactors |