Lipase‐Supported Metal–Organic Framework Bioreactor Catalyzes Warfarin Synthesis

Liu, Wan Ling; Yang, Ni Shin; Chen, Ya Ting; Lirio, Stephen; Wu, Chao‐Ming; Lin, Chia Her; Huang, Hsi Ya

doi:10.1002/chem.201405252

Cited by 109 publications

(59 citation statements)

References 39 publications

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“…Another non-covalent approach to surface functionalization involves partial infiltration of the biomacromolecule within the MOF pore network: e.g. Huang and Lin [19][20][21] immobilized Trypsin onto various MOFs by tagging the enzyme with NBD. 20 The NBD facilitates a strong host-guest interaction arising from a close match between the molecular dimensions of the dye and pore window of the MOF.…”

Section: Adsorptionmentioning

confidence: 99%

Metal–Organic Frameworks at the Biointerface: Synthetic Strategies and Applications

et al. 2017

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Many living organisms are capable of producing inorganic materials of precisely controlled structure and morphology. This ubiquitous process is termed biomineralization and is observed in nature from the macroscale (e.g., formation of exoskeletons) down to the nanoscale (e.g., mineral storage and transportation in proteins). Extensive research efforts have pursued replicating this chemistry with the overarching aims of synthesizing new materials of unprecedented physical properties and understanding the complex mechanisms that occur at the biological-inorganic interface. Recently, we demonstrated that a class of porous materials termed metal-organic frameworks (MOFs) can spontaneously form on protein-based hydrogels via a process analogous to natural matrix-mediated biomineralization. Subsequently, this strategy was extended to functional biomacromolecules, including proteins and DNA, which have been shown to seed and accelerate crystallization of MOFs. Alternative strategies exploit co-precipitating agents such as polymers to induce MOF particle formation thus facilitating protein encapsulation within the porous crystals. In these examples the rigid molecular architecture of the MOF was found to form a protective coating around the biomacromolecule offering improved stability to external environments that would normally lead to its degradation. In this way, the MOF shell mimics the protective function of a biomineralized exoskeleton. Other methodologies have also been explored to encapsulate enzymes within MOF structures, including the fabrication of polycrystalline hollow MOF microcapsules that preserve the original enzyme functionality over several batch reaction cycles. The potential to design MOFs of varied pore size and chemical functionality has underpinned studies describing the postsynthesis infiltration of enzymes into MOF pore networks and bioconjugation strategies for the decoration of the MOF outer surface, respectively. These methods and configurations allow for customized biocomposites. MOF biocomposites have been extended from simple proteins to complex biological systems including viruses, living yeast cells, and bacteria. Indeed, a noteworthy result was that cells encapsulated within a crystalline MOF shell remain viable after exposure to a medium containing lytic enzymes. Furthermore, the cells can adsorb nutrients (glucose) through the MOF shell but cease reproducing until the MOF casing is removed, at which point normal cellular activity is fully restored. The field of MOF biocomposites is expansive and rapidly developing toward different applied research fields including protection and delivery of biopharmaceuticals, biosensing, biocatalysis, biobanking, and cell and virus manipulation. This Account describes the current progress of MOFs toward biotechnological applications highlighting the different strategies for the preparation of biocomposites, the developmental milestones, the challenges, and the potential impact of MOFs to the field.

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Section: Adsorptionmentioning

confidence: 99%

Metal–Organic Frameworks at the Biointerface: Synthetic Strategies and Applications

et al. 2017

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“…However, this approach is far from being universal, as it entails two essential problems: (i) just a few (expensive and/or hard‐to‐prepare) MOF materials possess sufficiently large mesopores; and (ii) it is restricted to enzymes with small molecular dimensions that are able to be accommodated inside these pores . Nevertheless, very recently, some studies have opened the possibility of synthesizing enzyme‐MOF biocatalysts without the requirement of hosting the enzymes within the structural pores of the MOF material, through either post‐synthesis or in situ approaches. In other words, the formation of the enzyme‐MOF composites can now take advantage of the extraordinary structural and compositional versatility as well as hierarchical porosity of MOF materials due to the use of a huge variety of organic functional moieties, metal nature, particle size, synthesis conditions, etc …”

Section: Introductionmentioning

confidence: 99%

In situ and post‐synthesis immobilization of enzymes on nanocrystalline MOF platforms to yield active biocatalysts

Gascón

Castro-Miguel

Díaz-García

et al. 2017

J of Chemical Tech & Biotech

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BACKGROUND: Very recently, metal-organic framework (MOF) materials have been postulated as emerging supports to achieve solid-state enzyme-contained biocatalysts. In this work, post-synthesis and in situ strategies to immobilize -glucosidase and laccase on different MOF materials were studied. The MOF-based supports, i.e. MIL-53(Al), NH 2 -MIL-53(Al) and Mg-MOF-74, were prepared under soft and sustainable conditions (room temperature and pH values compatible with enzymatic activity), allowing development of the in situ strategy. RESULTS:In both post-synthesis and in situ approaches, the intercrystalline mesoporosity of the MOF-based support favored the immobilization efficiency or the specific activity. The latter expressed as units per milligram of immobilized enzyme was higher in the post-synthesis immobilization, whereas the biocatalysts prepared in situ gave much higher enzyme loading (over 85%) and lower enzyme leaching (around 5%). The in situ approach even worked in a non-aqueous (N,N-dimethylformamide) media in which the free enzyme was completely inactive. The immobilized enzymes are much larger than the structural pores of the MOFs. CONCLUSIONS: Enzymes can be efficiently immobilized on nanocrystalline MOFs prepared under soft and sustainable conditions despite the supports lacking large enough pores to host the enzymes. The in situ approach is very efficient capturing enzymes and preserving some of their activity even under adverse conditions. Electrophoresis test of enzyme retention in biocatalystsThe efficiency of the enzyme encapsulation was studied by means of SDS-PAGE electrophoresis. Since the solid samples are not suitable for electrophoresis, the enzyme was forced to leave the pores by the following procedure. First, the biocatalysts were suspended in the electrophoresis buffer solution (containing sodium dodecyl sulfate, mercaptoethanol, bromophenol blue, tris buffer pH 6.8 and glycerol) and boiled for 10 min. In such denaturing conditions including the split of disulfide bonds, the tertiary structure of the protein should be lost and the random coil chain should then be easily released from the pores. The supernatants of these suspensions were withdrawn and run in 10 % SDS-PAGE electrophoresis.

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“…Moreover, Lin and Huang's group demonstrated a novel porcine pancreatic lipase (PPL)@MOF bioreactor with three microporous MOFs (UiO-66(Zr), UiO-66-NH 2 (Zr) and carbonized MIL-53(Al)). [10] With simple vortex assisted enzyme adsorption, PPL was confirmed to be successfully adsorbed onto MOFs. The PPL@MOF bioreactor was used to facilitate the Michael addition reaction to yield warfarin, a common anticoagulant in the clinic, with an exceptional catalytic ability and reusability ( Figure 1B).…”

Section: Surface Immobilizationmentioning

confidence: 98%

Metal‐Organic Frameworks: A New Platform for Enzyme Immobilization

Kou

Shen

et al. 2020

ChemBioChem

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Metal‐organic frameworks (MOFs) with attractive properties such as high surface area, tunable porosity, designable functionality and excellent stability, have aroused great interest from researchers as the matrices for enzyme immobilization. Recently, several efficient strategies including surface immobilization, post‐synthetic infiltration and in situ encapsulation have been explored. MOF‐immobilized enzymes, named enzymes@MOFs, show remarkably enhanced stability and recyclability, accelerating cell‐free biocatalysis in diverse applications. This concept will impart the typical strategies for enzyme immobilization with MOFs, and their potential applications.

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Lipase‐Supported Metal–Organic Framework Bioreactor Catalyzes Warfarin Synthesis

Cited by 109 publications

References 39 publications

Metal–Organic Frameworks at the Biointerface: Synthetic Strategies and Applications

Metal–Organic Frameworks at the Biointerface: Synthetic Strategies and Applications

In situ and post‐synthesis immobilization of enzymes on nanocrystalline MOF platforms to yield active biocatalysts

Metal‐Organic Frameworks: A New Platform for Enzyme Immobilization

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