Monodispersed MOF-808 Nanocrystals Synthesized via a Scalable Room-Temperature Approach for Efficient Heterogeneous Peptide Bond Hydrolysis

Chemistry of Materials, Journal Year: 2021, Volume and Issue: 33(17), P. 7057 - 7066

Published: Aug. 30, 2021

Zr(IV)-based metal–organic frameworks (MOFs) such as the Zr(IV) trimesate MOF-808 are promising materials for catalytic applications. In this work, we report an aqueous solution-based room-temperature strategy to produce well-defined monodispersed nanocrystals down 35 nm with a high space-time yield, up 2516 kg/m3/day, and excellent crystallinity porosity. The resulting show remarkable colloidal dispersion during 1 day in wide range of nanoparticle concentrations. As result, colloidal-level exhibit highest rate selective peptide bond protein hydrolysis among reported MOFs. This result may open new opportunities highly efficient or using scalable nanocatalysts.

Language: Английский

---

Enzyme Catalyst Engineering toward the Integration of Biocatalysis and Chemocatalysis

Trends in biotechnology, Journal Year: 2021, Volume and Issue: 39(11), P. 1173 - 1183

Published: Feb. 5, 2021

Language: Английский

---

Nano-bio-interface engineering of metal-organic frameworks

Nano Today, Journal Year: 2021, Volume and Issue: 40, P. 101256 - 101256

Published: July 20, 2021

Language: Английский

---

Locking the Ultrasound-Induced Active Conformation of Metalloenzymes in Metal–Organic Frameworks

Journal of the American Chemical Society, Journal Year: 2022, Volume and Issue: 144(39), P. 17865 - 17875

Published: Sept. 8, 2022

Enhancing the enzymatic activity inside metal-organic frameworks (MOFs) is a critical challenge in chemical technology and bio-technology, which, if addressed, will broaden their scope energy, food, environmental, pharmaceutical industries. Here, we report simple yet versatile effective strategy to optimize biocatalytic by using MOFs rapidly "lock" ultrasound (US)-activated but more fragile conformation of metalloenzymes. The results demonstrate that up 5.3-fold 9.3-fold enhancement free MOF-immobilized enzymes could be achieved compared those without US pretreatment, respectively. Using horseradish peroxidase as model, molecular dynamics simulation demonstrates improved enzyme driven an opened gate heme active site, which allows efficient substrate binding enzyme. intact site confirmed solid-state UV-vis electron paramagnetic resonance, while US-induced change circular dichroism spectroscopy Fourier-transform infrared spectroscopy. In addition, biocomposites does not compromise stability upon heating or exposure organic solvent digestion cocktail. This rapid locking immobilization gives rise new possibilities for exploitation highly biocatalysts diverse applications.

Language: Английский

---

Covalent Organic Framework Based Crosslinked Porous Microcapsules for Enzymatic Catalysis

Angewandte Chemie International Edition, Journal Year: 2023, Volume and Issue: 62(33)

Published: June 13, 2023

Abstract The design of porous microcapsules with selective mass transfer and mechanical robustness for enzyme encapsulation is highly desired biocatalysis, yet the construction remains challenging. Herein, we report facile fabrication by assembling covalent organic framework (COF) spheres at interfaces emulsion droplets followed interparticle crosslinking. COF could offer an enclosed aqueous environment enzymes, size‐selective shells that allow fast diffusion substrates products while excluding larger molecules such as protease. Crosslinking not only enhances structural stability capsules but also imparts enrichment effects. enzymes encased in show enhanced activity durability media verified both batch reaction continuous‐flow reaction. a promising platform biomacromolecules.

Language: Английский

---

Construction of Covalent Organic Framework Capsule-Based Nanoreactor for Sensitive Glucose Detection

ACS Applied Materials & Interfaces, Journal Year: 2023, Volume and Issue: 15(7), P. 10158 - 10165

Published: Feb. 14, 2023

Enzyme immobilization is critical to boosting its application in various areas. Covalent organic frameworks (COFs) are ideal hosts for enzyme due their porous and predesignable structures. Nevertheless, the construction of COFs-based systems with high activity via existing methods (including covalent linkages channel entrapment) remains a considerable challenge. Herein, versatile approach was introduced encapsulate enzymes within hollow COF capsule (named enzyme@COF) using metal–organic ZPF-1(C8H11N4O4.5Zn), ZIF-8(C8H10N4Zn), ZIF-90(C8H6N4O2Zn)) as sacrificial templates. The obtained could not only facilitate efficient mass transfer enzymatic reactions but also protect against incompatible conditions, resulting enhanced stability encapsulated enzymes. Moreover, this offered an opportunity spatially organize multienzymes construct cascade system. For instance, glucose oxidase (GOx) cytochrome c (Cyt c) were coencapsulated GOx-Cyt cascade. integration GOx Cyt achieved ∼1.6-fold improvement catalytic than that free resultant c@COF successfully adopted nanoreactor sensitive determination serum. This work provided new insight into design systems.

Language: Английский

---

A Dynamic Defect Generation Strategy for Efficient Enzyme Immobilization in Robust Metal‐Organic Frameworks for Catalytic Hydrolysis and Chiral Resolution

Angewandte Chemie International Edition, Journal Year: 2023, Volume and Issue: 62(20)

Published: March 14, 2023

Enzyme immobilization has been demonstrated to be a favorable protocol for promoting the industrialization of bioactive molecules, but still with formidable challenge. Addressing this challenge, we create dynamic defect generation strategy enzyme by using dissociation equilibrium metal-organic frameworks (MOFs) mediated enzymes. Enzymes can act as "macro ligands" generate competitive coordination against original ligands, along release metal clusters MOFs defects, hence gradual transport enzymes from surface inside. Various efficiently immobilized in afford composites good enzymatic activities, protective performances and exceptional reusabilities. Moreover, multienzyme bioreactors capable efficient cascade reactions also generated. This study provides new opportunities construct highly biocatalysts incorporating different types

Language: Английский

---

Nanoconfinement‐Guided Construction of Nanozymes for Determining H₂O₂ Produced by Sonication

Angewandte Chemie International Edition, Journal Year: 2023, Volume and Issue: 62(12)

Published: Jan. 27, 2023

Nanomaterials with enzyme-like activities, termed as nanozymes, have found wide applications in various fields. It has been a long-term aim to rationally design and synthesize highly active nanozymes thus further improve their application performance. Guided by the nanoconfinement effect, we confine cytochrome c (Cyt c) within mesoporous metal-organic framework (MOF), PCN-222 nanoparticle (NP), forming protein/MOF hybrid nanozyme, Cyt c@PCN-222 NP. The confined exhibits around 3-4-fold higher peroxidase-like activity than free c. Due increase of c, NPs exhibit quite low limit detection (≈0.13 μM) towards H2 O2 . Sonication-induced formation water using lab-quipped ultrasonic cleaner can be sensitively probed, which suggests that -sensitive materials should carefully handled during utilization equipment. We speculate this strategy broaden our synthetic methodology for rational nanozymes.

Language: Английский

---

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Chem & Bio Engineering, Journal Year: 2024, Volume and Issue: 1(2), P. 99 - 112

Published: Feb. 8, 2024

Enzymes, as highly efficient biocatalysts, excel in catalyzing diverse reactions with exceptional activity and selective properties under mild conditions. Nonetheless, their broad applications are hindered by inherent fragility, including low thermal stability, limited pH tolerance, sensitivity to organic solvents denaturants. Encapsulating enzymes within metal–organic frameworks (MOFs) can protect them from denaturation these harsh environments. However, this often leads a compromised enzyme activity. In recent years, extensive research efforts have been dedicated enhancing enzymatic MOFs, leading the development of new enzyme–MOF composites that not only preserve catalytic potential but also outperform free counterparts. This Review provides comprehensive review on developments specific emphasis enhanced compared enzymes.

Language: Английский

---

Boosted Enzyme Activity via Encapsulation within Metal–Organic Frameworks with Pores Matching Enzyme Size and Shape

Advanced Science, Journal Year: 2024, Volume and Issue: 11(21)

Published: April 4, 2024

Abstract A novel and versatile approach called “physical imprinting” is introduced to modulate enzyme conformation using mesoporous materials, addressing challenges in achieving improved activity stability. Metal–organic frameworks with tailored mesopores, precisely matching size shape, are synthesized. Remarkably, enzymes encapsulated within these customized mesopores exhibit over 1670% relative compared free enzymes, maintaining outstanding efficiency even under harsh conditions such as heat, exposure organic solvents, wide‐ranging pH extremes from acidic alkaline, a digestion cocktail. After 18 consecutive cycles of use, the immobilized retain 80% their initial activity. Additionally, substantial increase catalytic efficiency, 14.1‐fold enhancement k cat / K M native enzymes. This among highest reported for The stability corroborated by solid‐state UV–vis, electron paramagnetic resonance, Fourier‐transform infrared spectroscopy, NMR spectroscopy. findings not only offer valuable insights into crucial role shape complementarity confined microenvironments but also establish new pathway developing solid carriers capable enhancing

Language: Английский

---