Construction of multiple enzyme metal–organic frameworks biocatalyst via DNA scaffold: A promising strategy for enzyme encapsulation

Song, Jiayi; He, Wenting; Shen, Hao; Zhou, Zixin; Li, Mengqi; Su, Ping; Yang, Yi

doi:10.1016/j.cej.2019.01.138

Cited by 83 publications

(55 citation statements)

References 44 publications

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“…[37] GOx and HRP ZIF-8 Glucose biosensor K m and k cat /K m was 0.27-fold lower and 9.9-fold higher than those of free enzymes; LOD of glucose: 0.4 μM. [38] CA, FDH, GDH, NADH Amine-MIL-101(Cr) and HKUST-1 CO 2 Reduction Compared to free enzymes, formate yield was 13.1-fold higher.…”

Section: Pcn-333 Cholesterol Detectionmentioning

confidence: 91%

“…A typical example of positional co-immobilization of multi-enzyme is cross-linking GOx and HRP by the customdesigned DNA. [38] The individual enzyme was integrated with single DNA strands, then the enzyme-DNA bioconjugates (GOx-linker 1 and HRP-linker 2) was cross-linked by Yscaffold DNA constructed from stoichiometric quantities of the DNA strands (Y1, Y2, and Y3), which are denoted as GOx/HRP@DNA. Different from the random co-immobilization, GOx and HRP were positioned in close proximity by specific DNA strands, whereas different conjugates (GOx-GOx, HRP-HRP, GOx-HRP) may occur in the random coimmobilization.…”

Section: Positional Co-immobilizationmentioning

confidence: 99%

Section: P E R S O N a L A C C O U N T T H E C H E M I C A L R E C O R Dmentioning

confidence: 99%

“…A typical example of positional co‐immobilization of multi‐enzyme is cross‐linking GOx and HRP by the custom‐designed DNA . The individual enzyme was integrated with single DNA strands, then the enzyme‐DNA bioconjugates (GOx‐linker 1 and HRP‐linker 2) was cross‐linked by Y‐scaffold DNA constructed from stoichiometric quantities of the DNA strands (Y1, Y2, and Y3), which are denoted as GOx/HRP@DNA.…”

Section: Multi‐enzyme Co‐immobilization Strategies In Mofsmentioning

confidence: 99%

“…Moreover, compared to the free enzymes, k cat /K m and K m were 9.9‐fold increased and 0.27‐fold decreased. Over 83 % catalytic activity of GOx/HRP@DNA@ZIF‐8 was well reserved after storage at 4 °C for 15 days, and more than 87 % of initial activity still preserved after 14 cycles . The results suggested that the positional co‐immobilized multi‐enzyme within MOF was promising in the application of biomedical engineering, biocatalysis and biotechnology, such as diagnosis of diseases in specific regions, cleanup of environmental pollution, decomposition of glucose on the surface of cancer cells, sensing of glucose and design of multifunctional biosensors.…”

Section: Multi‐enzyme Co‐immobilization Strategies In Mofsmentioning

confidence: 99%

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Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

Liang

2020

The Chemical Record

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Multi-enzyme cascade reactions are indispensable in biotechnology and many industrial (bio)chemical processes. However, most natural enzymes have poor stability and reusability, and tend to inactivate in toxic media or high temperature, which significantly limit their broader applications. Metal-organic frameworks (MOFs) are promising candidates for enzymes immobilization to produce nanocomposite structures that not only could shield the enzymes from harsh environments, but also facilitate selective diffusion of substrates and intermediates to the reactive site via their tailorable and ordered pore network. Multi-enzyme cascade reactions in MOFs have recently attracted considerable attention. This Personal Account discusses the different strategies for multi-enzyme-MOF interfaces and their cutting-edge applications from biosensing and catalytic nanomedicine to artificial/hybrid cells. At last, we provide a critical evaluation and future prospects to outline future research directions.

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Section: Pcn-333 Cholesterol Detectionmentioning

confidence: 91%

Section: Positional Co-immobilizationmentioning

confidence: 99%

Section: P E R S O N a L A C C O U N T T H E C H E M I C A L R E C O R Dmentioning

confidence: 99%

Section: Multi‐enzyme Co‐immobilization Strategies In Mofsmentioning

confidence: 99%

Section: Multi‐enzyme Co‐immobilization Strategies In Mofsmentioning

confidence: 99%

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Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

Liang

2020

The Chemical Record

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Biocatalytic Metal–Organic Frameworks: Prospects Beyond Bioprotective Porous Matrices

Liang

2020

Adv Funct Materials

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Biocatalytic metal-organic framework (MOF) composites, synthesized by interfacing MOFs with biocatalytic components, possess the unprecedented synergetic properties that is hard to achieve by the conventional strategies, represents one of the next-generation composite materials for diverse biotechnological applications. Until now , research on the applications of biocatalytic MOFs is still in its preliminary stage, with a wide variety of studies being focusing on the bioprotection role of MOFs. However, their diversity of building units, molecular-scale tunability, modular synthetic routes, and more detailed understanding of the heterogeneous MOF-biointerface could even lead to completely new applications and potentials beyond our current imagination. The most recent rapid advanced progress in biocatalytic MOFs present ground-breaking applications in smart and tunable biocatalysis, precision nanomedicine, vaccine and gene delivery, biosensing and nano-biohybrids. Herein, the general and advanced synthesis strategies for improving the materials properties of biocatalytic MOFs, from tuning biocatalytic activity to framework stability to synergistic properties with other materials, are summarized. Then, the latest state-of-the-art applications of the biocatalytic MOF systems and recent advanced developments that are shaping this emerging field are surveyed. Finally, to define promising research directions, a critical evaluation and future prospects for the potential applications of biocatalytic MOFs are provided.

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MOF‐Immobilized Two‐in‐One Engineered Enzymes Enhancing Activity of Biocatalytic Cascade for Tumor Therapy

Yang

Chen

et al. 2023

Adv Healthcare Materials

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Biocatalytic systems based on enzyme cascade reactions have attracted growing interest in the field of biocatalytic medicine. However, it is a major challenge to reasonably construct enzyme cascade reactions with high stability, selectivity, and catalytic efficiency for the in vivo biocatalytic application. Herein, two‐in‐one engineered glucose oxidase (GOx‐Fe0) is fabricated by a biomineralization strategy, through which a nanozyme (Fe0NP) is anchored within the inner cavity of GOx. Then, GOx‐Fe0 is immobilized in a pH‐sensitive metal–organic framework (MOF) zeolitic imidazolate framework‐8 (ZIF‐8) to establish a stable and effective MOF‐immobilized two‐in‐one engineered enzyme, GOx‐Fe0@ZIF‐8. In vitro studies show that GOx‐Fe0@ZIF‐8 exhibits excellent stability and high pH/glucose selectivity, and the shorter spacing between cascade enzymes can increase the cascade throughput and effectively improve the reaction efficiency of the enzyme cascade. In vivo experiments exhibit that GOx‐Fe0@ZIF‐8 solves the instability and systemic toxicity of free enzymes, and achieves deep tumor penetration and significant chemodynamic therapeutic efficacy through a pH/glucose‐selective enzyme cascade reaction in tumor site. Taken together, such an orchestrated enzyme engineering strategy can effectively improve enzyme stability, selectivity, and enzyme cascade reaction efficiency via chemical transformations, and also provide a promising strategy for the application of biocatalytic cascade reactions in vivo.

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Construction of multiple enzyme metal–organic frameworks biocatalyst via DNA scaffold: A promising strategy for enzyme encapsulation

Cited by 83 publications

References 44 publications

Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

Multi‐enzyme Cascade Reactions in Metal‐organic Frameworks

Biocatalytic Metal–Organic Frameworks: Prospects Beyond Bioprotective Porous Matrices

MOF‐Immobilized Two‐in‐One Engineered Enzymes Enhancing Activity of Biocatalytic Cascade for Tumor Therapy

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