One-pot synthesis of enzyme@metal–organic material (MOM) biocomposites for enzyme biocatalysis

Pan, Yanxiong; Li, Hui; Lenertz, Mary; Han, Yulun; Ugrinov, Angel; Kilin, Dmitri S.; Chen, Bingcan; Yang, Zhongyu

doi:10.1039/d1gc00775k

Cited by 29 publications

(18 citation statements)

References 52 publications

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“…In order to preserve catalytic activity, macromolecules have been added in some of these one-pot systems: mixing polyvinylpyrrolidone (PVP) with Cyt C prior to the immobilization process in ZIF-8 [32] to form a double layer to protect its activity and stability. A lignin derivative (DDVA) has also been used to co-precipitate enzymes with Ca 2+ or Zn 2+ to yield enzyme@MOM composites [41]. Additionally, Fe 3 O 4 has successfully been added to provide particles with magnetic properties such as in the one-pot synthesis involving 2-methylimidazole and zinc acetate with lipase from Candida rugosa in the MOF CRL/MNP@ZIF-8 [42].…”

Section: The Origins and Rising Dominance Of The Enzyme-supporting Mofmentioning

confidence: 99%

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

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The industrial use of enzymes generally necessitates their immobilization onto solid supports. The well-known high affinity of enzymes for metal-organic framework (MOF) materials, together with the great versatility of MOFs in terms of structure, composition, functionalization and synthetic approaches, has led the scientific community to develop very different strategies for the immobilization of enzymes in/on MOFs. This review focuses on one of these strategies, namely, the one-pot enzyme immobilization within sustainable MOFs, which is particularly enticing as the resultant biocomposite Enzyme@MOFs have the potential to be: (i) prepared in situ, that is, in just one step; (ii) may be synthesized under sustainable conditions: with water as the sole solvent at room temperature with moderate pHs, etc.; (iii) are able to retain high enzyme loading; (iv) have negligible protein leaching; and (v) give enzymatic activities approaching that given by the corresponding free enzymes. Moreover, this methodology seems to be near-universal, as success has been achieved with different MOFs, with different enzymes and for different applications. So far, the metal ions forming the MOF materials have been chosen according to their low price, low toxicity and, of course, their possibility for generating MOFs at room temperature in water, in order to close the cycle of economic, environmental and energy sustainability in the synthesis, application and disposal life cycle.

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Section: The Origins and Rising Dominance Of The Enzyme-supporting Mofmentioning

confidence: 99%

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

et al. 2021

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“…Metal–organic frameworks (MOFs) are advanced platforms for enzyme immobilization and have provided advancement in biocatalysis, biomedicine, and fundamental biophysics research. − Thus far, major efforts in enzyme@MOF research have been focused on optimizing the metal, ligand, aperture, and/or pores of MOFs to enhance enzyme protection (against the reaction medium), reusability (as a result of the ease of separation), and substrate selectivity and/or diffusivity. − , While preformed, highly stable, and crystalline MOFs are mostly applied to host relatively small enzymes with small substrates, “one-pot” synthesis via co-crystallization of large enzymes and/or enzyme clusters with metals and ligands in the aqueous phase (also known as biomimetic mineralization) has been shown to be effective in removing the size limitation of enzymes. ,− Recently, researchers including our team have shown the possibility of using co-precipitation to remove the size limitation of the substrate, so that the entrapped enzymes are partially exposed to the reaction medium and partially buried under the MOF crystal surfaces, − as demonstrated on zeolitic imidazolate frameworks (ZIFs) and recent Ca-based metal–organic materials (MOMs, an analogue of MOFs but with a one- or two-dimensional structure); ,− the exposed enzyme regions were also revealed using our developed biophysical tools. , Importantly, our enzyme@Ca-MOM composites can be formed in the enzyme-friendly, aqueous phase under ambient conditions, minimizing the enzyme loss during co-precipitation . The Ca-MOMs are also stable under both weakly acidic and basic conditions, allowing for biocatalysis under the optimal pH of the immobilized enzyme.…”

Section: Introductionmentioning

confidence: 99%

Expanding the “Library” of Metal–Organic Frameworks for Enzyme Biomineralization

Jordahl

Armstrong

et al. 2022

ACS Appl. Mater. Interfaces

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Metal–organic frameworks (MOFs) are advanced platforms for enzyme immobilization. Enzymes can be entrapped via either diffusion (into pre-formed MOFs) or co-crystallization. Enzyme co-crystallization with specific metals/ligands in the aqueous phase, also known as biomineralization, minimizes the enzyme loss compared to organic phase co-crystallization, removes the size limitation on enzymes and substrates, and can potentially broaden the application of enzyme@MOF composites. However, not all enzymes are stable/functional in the presence of excess metal ions and/or ligands currently available for co-crystallization. Furthermore, most current biomineralization-based MOFs have limited (acid) pH stability, making it necessary to explore other metal–ligand combinations that can also immobilize enzymes. Here, we report our discovery on the combination of five metal ions and two ligands that can form biocomposites with two model enzymes differing in size and hydrophobicity in the aqueous phase under ambient conditions. Surprisingly, most of the formed composites are single- or multiphase crystals, even though the reaction phase is aqueous, with the rest as amorphous powders. All 20 enzyme@MOF composites showed good to excellent reusability and were stable under weakly acidic pH values. The stability under weakly basic conditions depended upon the selection of enzyme and metal–ligand combinations, yet for both enzymes, 3–4 MOFs offered decent stability under basic conditions. This work initiates the expansion of the current “library” of metal–ligand selection for encapsulating/biomineralizing large enzymes/enzyme clusters, leading to customized encapsulation of enzymes according to enzyme stability, functionality, and optimal pH.

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“…In our recent discovery, we found that an enzyme can be partially exposed above the surface of metal–organic frameworks/materials (MOFs/MOMs) upon co-crystallization while being partially buried (and thus, protected) in the scaffolds; − here, MOMs are usually referred to as 1D or 2D structures, while MOFs are 3D frameworks according to a strict definition . This strategy can offer enhanced enzyme protection to a satisfying extent so that a reasonable number of reuse cycles can be achieved.…”

Section: Introductionmentioning

confidence: 99%

Cascade/Parallel Biocatalysis via Multi-enzyme Encapsulation on Metal–Organic Materials for Rapid and Sustainable Biomass Degradation

Pan

et al. 2021

ACS Appl. Mater. Interfaces

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Multiple-enzyme cooperation simultaneously is an effective approach to biomass conversion and biodegradation. The challenge, however, lies in the interference of the involved enzymes with each other, especially when a protease is needed, and thus, the difficulty in reusing the enzymes; while extracting/synthesizing new enzymes costs energy and negative impact on the environment. Here, we present a unique approach to immobilize multiple enzymes, including a protease, on a metal–organic material (MOM) via co-precipitation in order to enhance the reusability and sustainability. We prove our strategy on the degradation of starch-containing polysaccharides (require two enzymes to degrade) and food proteins (require a protease to digest) before the quantification of total dietary fiber. As compared to the widely adopted “official” method, which requires the sequential addition of three enzymes under different conditions (pH/temperature), the three enzymes can be simultaneously immobilized on the surface of our MOM crystals to allow for contact with the large substrates (starch), while MOMs offer sufficient protection to the enzymes so that the reusability and long-term storage are improved. Furthermore, the same biodegradation can be carried out without adjusting the reaction condition, further reducing the reaction time. Remarkably, the simultaneous presence of all enzymes enhances the reaction efficiency by a factor of ∼3 as compared to the official method. To our best knowledge, this is the first experimental demonstration of using aqueous-phase co-precipitation to immobilize multiple enzymes for large-substrate biocatalysis. The significantly enhanced efficiency can potentially impact the food industry by reducing the labor requirement and enhancing enzyme cost efficiency, leading to reduced food cost. The reduced energy cost of extracting enzymes and adjusting reaction conditions minimize the negative impact on the environment. The strategy to prevent protease damage in a multi-enzyme system can be adapted to other biocatalytic reactions involving proteases.

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One-pot synthesis of enzyme@metal–organic material (MOM) biocomposites for enzyme biocatalysis

Abstract: Metal-Organic Frameworks/Materials (MOFs/MOMs) are advanced enzyme immobilization platforms that improve biocatalysis, materials science, and protein biophysics. A unique way to immobilize enzymes is co-crystallization/co-precipitation, which removes the limitation on enzyme/substrate...

Cited by 29 publications

References 52 publications

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Sustainable One-Pot Immobilization of Enzymes in/on Metal-Organic Framework Materials

Expanding the “Library” of Metal–Organic Frameworks for Enzyme Biomineralization

Cascade/Parallel Biocatalysis via Multi-enzyme Encapsulation on Metal–Organic Materials for Rapid and Sustainable Biomass Degradation

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