2021
DOI: 10.1039/d1tc00407g
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Stable MOF@enzyme composites for electrochemical biosensing devices

Abstract: Naturally occurring enzymes are highly selective and efficient catalysts but given their intricate and fragile structure, wide application of their extraordinary catalytic potential in industrial and biomedical settings is highly...

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Cited by 33 publications
(28 citation statements)
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“…Peroxidases can be deactivated by hydrogen peroxide [46] and laccases by mediators [47] as well as products [48] . Immobilization of enzymes with MOFs has been shown extensively to protect enzymes under conditions that deviate from normal operating parameters including temperature and variations in pH [49–56] . Enzymes can be either immobilized onto the MOF surface or loaded into the MOF by infiltration within the limits of loading capacity of each of these techniques [57–68] .…”
Section: Breakdown and Mineralizationmentioning
confidence: 99%
See 1 more Smart Citation
“…Peroxidases can be deactivated by hydrogen peroxide [46] and laccases by mediators [47] as well as products [48] . Immobilization of enzymes with MOFs has been shown extensively to protect enzymes under conditions that deviate from normal operating parameters including temperature and variations in pH [49–56] . Enzymes can be either immobilized onto the MOF surface or loaded into the MOF by infiltration within the limits of loading capacity of each of these techniques [57–68] .…”
Section: Breakdown and Mineralizationmentioning
confidence: 99%
“… [48] Immobilization of enzymes with MOFs has been shown extensively to protect enzymes under conditions that deviate from normal operating parameters including temperature and variations in pH. [ 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 ] Enzymes can be either immobilized onto the MOF surface or loaded into the MOF by infiltration within the limits of loading capacity of each of these techniques. [ 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 ] A more advanced technique is biomimetic mineralization, [69] wherein the MOF self‐assembles around the enzyme (de novo encapsulation) and has been proven to significantly enhance stability (Figure 4 c).…”
Section: Breakdown and Mineralizationmentioning
confidence: 99%
“…Due to the weak coordinative bond between the metal and constituent ligand, the primary MOFs used as catalysts have limited mechanical, thermal, and chemical resistance [ 16 , 17 ]. Today, a type of functional materials (e.g., metal nanoparticles [NPs] [ [18] , [19] , [20] , [21] ], quantum dots [QDs] [ 22 , 23 ], polyoxometalates [POMs] [ 24 , 25 ], molecular species [ 26 , 27 ], enzymes [ 28 , 29 ], silica [ 30 , 31 ], and polymers [ [32] , [33] , [34] ] have been integrated with MOFs to generate MOF composites/hybrids composed. These composites have unique chemical and physical properties such as catalysis or peroxidase-like activity, optical, electrical, and magnetic properties, and mechanical strength [ 18 ].…”
Section: Introductionmentioning
confidence: 99%
“…Aqueous environments represent especially challenging conditions for MOFs because of the potential of the hydrolytic cleavage of weak coordination bonds which constitute the MOF backbone . Reports have described the low hydrolytic stability ,, of MOFs, but these aspects are generally not considered in detail when examining enzyme immobilization. , The stability of MOFs in water is determined by the strength of the metal-linker coordination bonds and the level of saturation of metal sites, resulting in different MOFs displaying varying hydrolytic stability. Additionally, the composition of buffers commonly used in enzymatic reactions needs to be considered as the buffer can affect the MOF’s structural integrity, in particular, by disturbing the coordination bonds. ,, Breakdown of the MOF structure in buffered solutions ,, is a key challenge facing the use of MOFs for the immobilization of enzymes, as buffers are required for enzymatic activity.…”
Section: Introductionmentioning
confidence: 99%