Abstract:The artificial engineering of an enzyme's structural conformation to enhance its activity is highly desired and challenging. Anisotropic reticular chemistry, best illustrated in the case of multivariate metal−organic frameworks (MTV-MOFs), provides a platform to modify a MOF's pore and inner-surface with functionality variations on frameworks to optimize the interior environment and to enhance the specifically targeted property. In this study, we altered the functionality and ratio of linkers in zeolitic imida… Show more
“…State-of-the-art MOFs are complex/multicomponent/multivariate MOFs prepared through various strategies, 131,320,332,334,336,337,351–360 possessing multiple active sites, which target synergistic/cooperative photocatalysis and catalysis and advanced tandem reactions.…”
Section: Classification Of Porous Materials and Their Active Sites Fo...mentioning
confidence: 99%
“…338 Photocatalyst-based MOF systems possess plentiful reactive sites and increased electron-hole pair lifetime (decrease in photogenerated charge recombination rate) and charge mobility compared to the traditional semiconductors. 340 State-of-the-art MOFs are complex/multicomponent/multivariate MOFs prepared through various strategies, 131,320,332,334,336,337,[351][352][353][354][355][356][357][358][359][360] possessing multiple active sites, which target synergistic/cooperative photocatalysis and catalysis and advanced tandem reactions.…”
Section: Strategies For Introducing Catalytic Moietiesmentioning
The review summarizes the state-of-the-art of C–H active transformations over crystalline and amorphous porous materials as new emerging heterogeneous (photo)catalysts.
“…State-of-the-art MOFs are complex/multicomponent/multivariate MOFs prepared through various strategies, 131,320,332,334,336,337,351–360 possessing multiple active sites, which target synergistic/cooperative photocatalysis and catalysis and advanced tandem reactions.…”
Section: Classification Of Porous Materials and Their Active Sites Fo...mentioning
confidence: 99%
“…338 Photocatalyst-based MOF systems possess plentiful reactive sites and increased electron-hole pair lifetime (decrease in photogenerated charge recombination rate) and charge mobility compared to the traditional semiconductors. 340 State-of-the-art MOFs are complex/multicomponent/multivariate MOFs prepared through various strategies, 131,320,332,334,336,337,[351][352][353][354][355][356][357][358][359][360] possessing multiple active sites, which target synergistic/cooperative photocatalysis and catalysis and advanced tandem reactions.…”
Section: Strategies For Introducing Catalytic Moietiesmentioning
The review summarizes the state-of-the-art of C–H active transformations over crystalline and amorphous porous materials as new emerging heterogeneous (photo)catalysts.
“…Thus, the hydrogen bonds of the framework could be adequately adjusted to be strong enough to interact with enzyme surface and generate an optimized conformation, albeit leaving untouched the structure of the buried catalytic triad. Ultimately, this allowed maintaining 99% enantiomeric excess of the products in several kinetic resolution reactions that were evaluated [136]. Within the same scope, Ruiz and co-workers, showed that depending on the type of carrier, and concomitantly immobilization method used and corresponding enzyme-enzyme and enzyme-surface interactions, the catalytic features of a psychrophilic lipase were modified.…”
Section: Carrier Composition and Immobilization Methodsmentioning
Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.
“…Considerable efforts have been devoted to constructing efficient enzyme‐immobilization systems through strategies such as adsorption, covalent bonding, crosslinking, using various materials (e.g., polymer, silica, metal oxide) as the matrix [10–18] . However, vast limitations still remain in this field, such as encapsulation of large‐size enzymes, substrate/product transfer issues caused by nonporous carriers, leaching or conformational change of enzymes during the immobilization process [19–22] . It is also of great challenge to elaborately design the immobilization systems to adapt the characteristics of enzyme/reaction or expediently fabricate the immobilized biocatalysts on a large scale [23] .…”
Enzyme immobilization is essential to the commercial viability of various critical large-scale biocatalytic processes. However, challenges remain for the immobilization systems, such as difficulties in loading large enzymes, enzyme leaching, and limitations for large-scale fabrication. Herein, we describe a green and scalable strategy to prepare high-performance biocatalysts through in situ assembly of enzymes with covalent organic frameworks (COFs) under ambient conditions (aqueous solution and room temperature). The obtained biocatalysts have exceptional reusability and stability and serve as efficient biocatalysts for important industrial reactions that cannot be efficiently catalyzed by free enzymes or traditional enzyme immobilization systems. Notably, this versatile enzyme immobilization platform is applicable to various COFs and enzymes. The reactions in an aqueous solution occurred within a short timeframe (ca. 10-30 min) and could be scaled up readily (ca. 2.3 g per reaction).
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