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

Feng, Yifan; Shi, Ruixuan; Yang, Ming-Wei; Zheng, Yulong; Zhang, Zhenjie; Chen, Yao

doi:10.1002/anie.202302436

Cited by 20 publications

(10 citation statements)

References 71 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several enzymes, including lipase, catalase, and glucose oxidase, have been successfully immobilized in UiO-66, showing good enzymatic activities and stability. Furthermore, this approach offers broad applicability, presenting a cost-effective alternative to the ball milling method for industrial MOF-based composite production …”

Section: Applications Of Enzyme–mof Compositesmentioning

confidence: 99%

“…Furthermore, this approach offers broad applicability, present-ing a cost-effective alternative to the ball milling method for industrial MOF-based composite production. 67 Recently, a particular focus on the fabrication of MOF− enzyme-composite-based devices has emerged. 105 Bell et al reported a facile method of interfacial crystallization to integrate enzyme-encapsulated MOF crystals onto the reactive shell-side of hollow fiber membranes.…”

Section: Applications Of Enzyme−mof Compositesmentioning

confidence: 99%

See 1 more Smart Citation

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Weng,

Chen,

Hui

et al. 2024

Chem Bio Eng.

View full text Add to dashboard Cite

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 their inherent fragility, including low thermal stability, limited pH tolerance, and sensitivity to organic solvents and denaturants. Encapsulating enzymes within metal−organic frameworks (MOFs) can protect them from denaturation in these harsh environments. However, this often leads to a compromised enzyme activity. In recent years, extensive research efforts have been dedicated to enhancing enzymatic activity within MOFs, leading to the development of new enzyme− MOF composites that not only preserve their catalytic potential but also outperform their free counterparts. This Review provides a comprehensive review on recent developments in enzyme−MOF composites with a specific emphasis on their enhanced enzymatic activity compared to free enzymes.

show abstract

Section: Applications Of Enzyme–mof Compositesmentioning

confidence: 99%

Section: Applications Of Enzyme−mof Compositesmentioning

confidence: 99%

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Weng,

Chen,

Hui

et al. 2024

Chem Bio Eng.

View full text Add to dashboard Cite

show abstract

“…Our other work used proteins as “hoes” to infiltrate enzymes into the structure by “picking” the structure of the MOF. Enzymes serve as macro ligands to generate competitive coordination against original ligands, along with the release of metal clusters of MOFs to generate defects, facilitating the transport of enzymes from the surface to the structure’s interior . In the sacrificial templating strategy, we selected MOFs such as ZIF-90 and ZPF-2 that can efficiently load and protect various biologically active macromolecules while remaining digestible under mild acidic conditions as cores.…”

Section: Enzyme-immobilization Strategiesmentioning

confidence: 99%

Integration of Enzyme and Covalent Organic Frameworks: From Rational Design to Applications

Qiao,

Jin,

Zuo

et al. 2023

Acc. Chem. Res.

Self Cite

View full text Add to dashboard Cite

Metrics & MoreArticle Recommendations CONSPECTUS: Manufacturing is undergoing profound transformations, among which green biomanufacturing with low energy consumption, high efficiency, and sustainability is becoming one of the major trends. However, enzymes, as the "core chip" of biomanufacturing, are often handicapped in their application by their high cost, low operational stability, and nonreusability. Immobilization of enzymes is a technology that binds or restricts enzymes in a certain area with solid materials, allows them to still carry out their unique catalytic reaction, and allows them to be recycled and reused. Compared with free enzymes, immobilized enzymes boast numerous advantages such as enhanced storage stability, ease of separation, reusability, and controlled operation. Currently, commonly used supports for enzyme immobilization (e.g., mesoporous silica, sol−gel hydrogels, and porous polymer) can effectively improve enzyme stability and reduce product inhibition. However, they still face drawbacks such as potential leaching or conformational change during immobilization and poor machining performance. Especially, most enzyme carrier solid materials possess disordered structures, inevitably introducing deficiencies such as low loading capacity, hindered mass transfer, and unclear structure−property relationships. Additionally, it remains a notable challenge to meticulously design immobilization systems tailored to the specific characteristics of enzyme/reaction. Therefore, there is a significant demand for reliable solid materials to overcome the above challenges. Crystalline porous materials, particularly covalent organic frameworks (COFs), have garnered significant interest as a promising platform for immobilizing enzymes due to their unique properties, such as their crystalline nature, high porosity, accessible active sites, versatile synthetic conditions, and tunable structure. COFs create a stabilizing microenvironment that protects enzymes from denaturation and significantly enhances reusability. Nevertheless, some challenges still remain, including difficulties in loading large enzymes, reduced enzyme activities, and the limited functionality of carriers. Therefore, it is essential to develop innovative carriers and novel strategies to broaden the methods of immobilizing enzymes, enabling their application across a more diverse array of fields.The integration of enzymes with advanced porous materials for intensified performance and diverse applications is still in its infancy, and our group has done a series of pioneering works. This Account presents a comprehensive overview of recent research progress made by our group, including (i) the development of innovative enzyme immobilization strategies utilizing COFs to make the assembly and integration of enzymes and carriers more effective; (ii) rational design and construction of functional carriers for enzyme immobilization using COFs; and (iii) extensions of immobilized enzyme applications based on COFs from industrial catalysis to biomedic...

show abstract

“…Super-resolution microscopy (SRM) represents one of the most used standard methods for three-dimensional biological imaging, especially with the development of new types of fluorophores (such as Alexa Fluor, ATTO, and Cy dyes) that have high quantum yields, high photostability, and more importantly, minimal effects on labeled biomolecules. − Chen and co-workers used structured illumination microscopy (SIM) to reveal the dynamic defect generation strategy of enzymes infiltrating onto UiO-66 . Yet, SIM can only obtain a spatial resolution of ∼120 nm by mathematical deconvolution of interference patterns .…”

Section: Introductionmentioning

confidence: 99%

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Liu,

Cui,

et al. 2024

J. Am. Chem. Soc.

View full text Add to dashboard Cite

Protein@metal−organic frameworks (P@MOFs) prepared by coprecipitation of protein, metal ions, and organic ligands represent an effective method for protein stabilization with a wide spectrum of applications. However, the formation mechanism of P@MOFs via the coprecipitation process and the reason why proteins can retain their biological activity in the frameworks with highly concentrated metal ions remain unsettled. Here, by a combined methodology of single molecule localization microscopy and clustering analysis, we discovered that in this process enzyme molecules form clusters with metal ions and organic ligands, contributing to both the nucleation and subsequent crystal growth. We proposed that the clusters played an important role in the retention of overall enzymatic activity by sacrificing protein molecules on the cluster surface. This work offers fresh perspectives on protein behaviors in the formation of P@MOFs, inspiring future endeavors in the design and development of artificial bionanocomposites with high biological activities.

show abstract

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

Cited by 20 publications

References 71 publications

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Boosting Enzyme Activity in Enzyme Metal–Organic Framework Composites

Integration of Enzyme and Covalent Organic Frameworks: From Rational Design to Applications

Direct Imaging of Protein Clusters in Metal–Organic Frameworks

Contact Info

Product

Resources

About