Kinetic enhancement in high-activity enzyme complexes attached to nanoparticles

Malanoski, Anthony P.; Breger, Joyce C.; Brown, Carl W.; Deschamps, Jeffrey R.; Susumu, Kimihiro; Oh, Eunkeu; Anderson, George P.; Walper, Scott A.; Medintz, Igor L.

doi:10.1039/c7nh00052a

Cited by 22 publications

(38 citation statements)

References 43 publications

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“…These results indicate that ZnO caused a mixed inhibition of the CAT enzyme, which indicate that ZnO could combine with the enzyme molecules additionally the enzyme-substrate-complex. The increase in K cat of CAT was confirmed in previous reports by Malanoski et al 54 who concluded that the ZnO-NPs-enzyme complexes did not depend on the shifting of products to the surface of ZnO-NPs and the enzyme-complexes were directly influenced by ZnO-NPs engagement.…”

Section: Discussionsupporting

confidence: 84%

“…In the case of 10 μg mL −1 ZnO-BPs, the increase in the K m value and an insignificant change in V max may reveal that ZnO-BPs have an affinity for the active site of APX enzyme. The increase in the K cat of APX enzyme under 10 μg mL −1 ZnO-BPs despite decreased activity indicates reduced product dissociation from the enzyme-substrate complex 54 . The increase of K m , V max , and K cat of APX under 150 μg mL −1 ZnO-BPs indicate that the enzyme did not obey the Michaelis-Menten equation.…”

Section: Discussionmentioning

confidence: 99%

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Impacts of zinc oxide nano and bulk particles on redox-enzymes of the Punica granatum callus

Farghaly

Radi

Al-Kahtany

2020

Sci Rep

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The structure and function of cellular membranes were sustained by redox-enzymes. We studied the interaction between the oxidative stress caused by excessive accumulation of ZnO-nanoparticles (ZnO-NPs) in plants and the role of redox-enzymes that can alleviate this stress. The crude callus extract from pomegranate, which was treated with 0, 10, and 150 µg mL−1 ZnO-NPs or bulk particles (ZnO-BPs), was applied to study the activity and kinetics of redox-enzymes. The elevated ZnO-NPs, enhanced the lipoxygenase and polyphenol oxidase activity, while the ZnO-BPs did not modify them. The activities of superoxide dismutase, catalase, and phenylalanine ammonia-lyase were induced under ZnO-NPs or BPs treatments, whilst the opposite trend of peroxidase was observed. Ascorbate peroxidase activity increased under ZnO-NPs treatments but decreased under ZnO-BPs. The kinetics activity of enzymes showed changes under different levels of NPs and BPs. Additionally, NPs or BPs treatments reduced the uptake of copper, iron, magnesium, but increased zinc accumulation in callus tissues. Meanwhile, these treatments enhanced the accumulation of manganese ions but did not affect the accumulation of potassium and phosphorous in ZnO-NPs or BPs-stressed calli. Collectively, these results gave a quantitative evaluation of the competition of zinc and other minerals on the carriers, and in addition, they provided a basis for how to control ZnO-NPs or BPs toxicity via redox-enzymes.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Impacts of zinc oxide nano and bulk particles on redox-enzymes of the Punica granatum callus

Farghaly

Radi

Al-Kahtany

2020

Sci Rep

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“…25,26,29,32,34 Although the phenomena of scaffolding-induced catalytic enhancement has been widely observed, a full understanding of its underlying mechanisms is still lacking. 36 Such fundamental knowledge is vital for developing artificial scaffolded enzymatic systems that display improved performances, in order to engineer more efficient bioreactors, more sensitive biosensors, or more powerful biofuel cells. 4,10,[37][38][39] To this aim, model, organized, mono-and multi-components enzymatic systems have to be assembled onto well-defined nanoscaffolds and their catalytic behavior thoroughly studied.…”

Section: Introductionmentioning

confidence: 99%

Probing the Enzymatic Activity of Individual Biocatalytic fd-Viral Particles by Electrochemical-Atomic Force Microscopy

et al. 2020

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Surface-immobilized fd bacteriophage particles are used as scaffolds to coassemble the redox enzyme quinoprotein glucose dehydrogenase, PQQ-GDH, and its cosubstrate, PEG-tethered ferrocene. Individual decorated fd phages are visualized and simultaneously functionally interrogated by Mt/AFM-SECM microscopy, an in-situ local probe correlative imaging technique, combining atomic force (AFM) and electrochemical (SECM) microscopy in a mediator tethered (Mt) configuration. The statistical distribution of catalytic activity across the fd population is resolved, and the correlation between the functional properties of the phages and their actual dimensions assessed. Moreover, achievement of sub-particle resolution allows the enzymatic activity of individual viruses to be spatially mapped, revealing a highly active region located in the middle of the filamentous fd-scaffold. Quantitative modeling shows that this "catalytic hot-spot" arises from the interplay between charge transport by electron hopping between ferrocene moieties along the viral particles, and enzymatic catalysis. The developed model also enables complete analysis of GDH kinetics at the single bioscaffold scale, revealing differences in the functional behavior of the biocatalytic viral particles when addressed at the ensemble or at the single particle scale.

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“…Several common applications utilizing QDs have emerged including theranostics, cellular imaging, in vitro and in vivo biosensing, and photodetection. Among the biological applications of QDs, one of the most promising is their bioconjugation to enzymes where their increase in study has been in part due to their recently-established relationship in the enhancement in activity for various enzymes, including beta-galactosidase [40,89], alkaline phosphatase [41], trypsin [90], phosphotriesterase [39], and others.…”

Section: Enzyme Immobilization On Qdsmentioning

confidence: 99%

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

et al. 2020

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Nanoparticle scaffolds can impart multiple benefits onto immobilized enzymes including enhanced stability, activity, and recoverability. The magnitude of these benefits is modulated by features inherent to the scaffold–enzyme conjugate, amongst which the size of the nanoscaffold itself can be critically important. In this review, we highlight the benefits of enzyme immobilization on nanoparticles and the factors affecting these benefits using quantum dots and gold nanoparticles as representative materials due to their maturity. We then review recent literature on the use of these scaffolds for enzyme immobilization and as a means to dissect the underlying mechanisms. Detailed analysis of the literature suggests that there is a “sweet-spot” for scaffold size and the ratio of immobilized enzyme to scaffold, with smaller scaffolds and lower enzyme:scaffold ratios generally providing higher enzymatic activities. We anticipate that ongoing studies of enzyme immobilization onto nanoscale scaffolds will continue to sharpen our understanding of what gives rise to beneficial characteristics and allow for the next important step, namely, that of translation to large-scale processes that exploit these properties.

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Kinetic enhancement in high-activity enzyme complexes attached to nanoparticles

Abstract: Accumulating studies by many groups have found consistent enhancement in a wide variety of enzyme activities when they are displayed around nanoparticles.

Cited by 22 publications

References 43 publications

Impacts of zinc oxide nano and bulk particles on redox-enzymes of the Punica granatum callus

Impacts of zinc oxide nano and bulk particles on redox-enzymes of the Punica granatum callus

Probing the Enzymatic Activity of Individual Biocatalytic fd-Viral Particles by Electrochemical-Atomic Force Microscopy

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

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