A bifunctional metal organic framework of type Fe(III)-BTC for cascade (enzymatic and enzyme-mimicking) colorimetric determination of glucose

Zhao, Zhenghong; Pang, Jifeng; Liu, Wenren; Lin, Tianran; Ye, Fanggui; Zhao, Shulin

doi:10.1007/s00604-019-3416-7

Cited by 64 publications

(29 citation statements)

References 32 publications

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“…Among the known MOFs, use of semiamorphous Fe-BTC as a protein support has been relatively prolific [1,12,39,70,81]. As the in situ methodology is not sensitive to the size of the support pores, nor does the size of the enzyme limit the preparation of an active biocatalyst, this approach has been extended to a vast range of enzymes with different molecular weights [12,39], including laccase (LAC), lipase (LIP), alcohol dehydrogenase, e (ADH), glucose oxidase (GOx) and halophilic HvADH2, among others.…”

Section: Semiamorphous Fe-btcmentioning

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: Semiamorphous Fe-btcmentioning

confidence: 99%

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

et al. 2021

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“…[3][4][5] Recently, MOFs have been explored for their potential use in drug delivery, bio-storage and bio-catalysis. [6][7][8][9][10] For example, MOFs can act as protective hosts to preserve enzymes and active pharmaceutical ingredients (APIs) from biological degradation induced by temperature, solvents and proteolytic agents. [11][12][13][14][15] Zeolitic imidazolate framework-8 (ZIF-8), composed of tetrahedral Zn 2+ ions linked by 2-methylimidazolate (mIM) ligands, is one of the most studied MOF carriers.…”

Section: Introductionmentioning

confidence: 99%

Degradation of ZIF-8 in phosphate buffered saline media

et al. 2019

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“…ZIF-8, ZIF-90) 17, 19 and a few other MOFs (e.g. GOx@Fe-BTC (BTC = 1,3,5-benzenetricarboxylic acid)), 98 other biocompatible polymers and MOFs could be used to expand this research. The addition of a base to the reaction mixture can also promote the formation of MOF-based biocomposites.…”

Section: Additivesmentioning

confidence: 99%

Metal–Organic Framework-Based Enzyme Biocomposites

et al. 2021

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Due to their efficiency, selectivity, and environmental sustainability, there are significant opportunities for enzymes in chemical synthesis and biotechnology. However, as the three-dimensional active structure of enzymes is predominantly maintained by weaker non-covalent interactions, thermal, pH and chemical stressors can modify or eliminate activity. Metal-organic Frameworks (MOFs), which are extended porous network materials assembled by a bottom-up building block approach from metal-based nodes and organic linkers, can be used to afford protection to enzymes. The self-assembled structures of MOFs can be used to encase an enzyme in a process called encapsulation when the MOF is synthesized in the presence of the biomolecule. Alternatively, enzymes can be infiltrated into mesoporous MOF structures or surface bound via covalent or non-covalent processes. Integration of MOF materials and enzymes in this way affords protection and allows the enzyme to maintain activity in challenge conditions (e.g. denaturing agents, elevated temperature, non-native pH and organic solvents). In addition to forming simple enzyme/MOF biocomposites, other materials can be introduced to the composites to improve recovery or facilitate advanced applications in sensing and fuel cell technology. This review canvasses enzyme protection via encapsulation, pore infiltration and surface adsorption and summarizes strategies to form multi-component composites. Also, given that enzyme/MOF biocomposites straddle materials chemistry and enzymology, this review provides an assessment of the characterization methodologies used for MOF-immobilized enzymes and identifies some key parameters to facilitate development of the field. CONTENTSMOF-based enzyme biocomposite compositions and the concept of encapsulation 3.MOF-based enzyme biocomposites formed via encapsulation 3.1.Templating methods 3.2.One-pot embedding (non-templated) 3.3.Parameters influencing the chemistry of enzyme@MOF biocomposites 3.3.1. Additives 3.3.2.Enzyme suface chemistry 3.3.3.MOF precusors and structures 3.4.Alternative synthesis strategies 4.Infiltration (post insertion of enzymes in preformed MOFs) 4.1.Early results and the advantages of MOFs for infiltration 4.2.Tuning the framework structure in infiltrated enzyme@MOF biocomposites 4.3.Towards applications of infiltrated enzyme@MOFs 5.Surface bound enzymes 5.1. Immobilization via physical adsorption 5.2. Immobilization via coordinate bonds 5.3. Immobilization via covalent bonding 5.4. Enzymatic activity upon surface-immobilization 6. Multicomponent biocomposites 7. Characterization of MOF immobilized enzymes 7.1. Overview 7.2. Key immobilization parameters 7.3. One-pot enzyme MOF formation 7.4. Highlights of MOF-immobilized enzyme performance 7.4.1. Experimental determination of key immobilization parameters 7.4.1.1. Determination of protein concentrations 7.4.1.2. Activity determination 7.4.2. Advanced characterization of immobilized enzymes 7.4.2.1. Apparent enzyme kinetics 7.4.2.2. Structural analysis and localization o...

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A bifunctional metal organic framework of type Fe(III)-BTC for cascade (enzymatic and enzyme-mimicking) colorimetric determination of glucose

Cited by 64 publications

References 32 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

Degradation of ZIF-8 in phosphate buffered saline media

Metal–Organic Framework-Based Enzyme Biocomposites

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