BioNano engineered hybrids for hypochlorous acid generation

Campbell, Alan S.; Dong, Chenbo; Dordick, Jonathan S.; Dinu, Cerasela Zoica

doi:10.1016/j.procbio.2013.06.011

Cited by 29 publications

(38 citation statements)

References 48 publications

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“…Contrary to that, increased protein−protein interactions caused by a less curved surface could result in a more dramatic activity loss over time and in a harsh environment. 11,12,36,63 The nanosupport's curvature trend was not confirmed for the enzyme immobilized onto SWCNTs relative to the enzyme immobilized onto MWCNTs; in particular, SBP showed the highest enzyme activity at the MWCNTs interface which has a larger radius of curvature than that of the SWCNTs. The apparent discrepancy in the reported results is due to the bio− nano interface being also influenced by the enzyme structure and its surface energy.…”

Section: ■ Materials and Methodsmentioning

confidence: 90%

“…However, upon such incubation, the remaining immobilized enzyme lost about 70% of its initial activity possibly due to the accelerated covalent multipoint attachment. 58 Enzyme catalytic behavior at the different CMAT nanointerfaces was assessed under varying concentrations of hydrogen peroxide (Figure 3b−d); the kinetic parameters V max (i.e., the maximum rate of reaction), K m (i.e., Michaelis−Menten constant), and k cat (i.e., enzyme turnover) were calculated using nonlinear regression 36,59 and compared with the kinetic parameters of the free enzyme in solution ( Table 1). The V max of SBP physically immobilized onto MWCNTs decreased by 87%, while the V max of the SBP immobilized onto GON decreased by about 98% relative to V max of free enzyme in solution.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Enzyme Catalytic Efficiency: A Function of Bio–Nano Interface Reactions

Campbell

Dong

Meng

et al. 2014

ACS Appl. Mater. Interfaces

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Biocatalyst immobilization onto carbon-based nanosupports has been implemented in a variety of applications ranging from biosensing to biotransformation and from decontamination to energy storage. However, retaining enzyme functionality at carbon-based nanosupports was challenged by the non-specific attachment of the enzyme as well as by the enzyme-enzyme interactions at this interface shown to lead to loss of enzyme activity. Herein, we present a systematic study of the interplay reactions that take place upon immobilization of three pure enzymes namely soybean peroxidase, chloroperoxidase, and glucose oxidase at carbon-based nanosupport interfaces. The immobilization conditions involved both single and multipoint single-type enzyme attachment onto single and multi-walled carbon nanotubes and graphene oxide nanomaterials with properties determined by Fourier transform infrared spectroscopy (FTIR), energy dispersive X-ray analysis (EDX), scanning electron microscopy (SEM), and atomic force microscopy (AFM). Our analysis showed that the different surface properties of the enzymes as determined by their molecular mapping and size work synergistically with the carbon-based nanosupports physico-chemical properties (i.e., surface chemistry, charge and aspect ratios) to influence enzyme catalytic behavior and activity at nanointerfaces. Knowledge gained from these studies can be used to optimize enzyme-nanosupport symbiotic reactions to provide robust enzyme-based systems with optimum functionality to be used for fermentation, biosensors, or biofuel applications.

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Section: ■ Materials and Methodsmentioning

confidence: 90%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Enzyme Catalytic Efficiency: A Function of Bio–Nano Interface Reactions

Campbell

Dong

Meng

et al. 2014

ACS Appl. Mater. Interfaces

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“…Immobilization onto nanosupports such as nanotubular aluminosilicate (71), graphene oxide (72), carbon nanotubes (73)(74)(75), graphene oxide sheets (74), nanodiamonds (76), and metal-oxide particles (77), was achieved either through physical or chemical means or through encapsulation into a gel (78) or membrane (79,80). Optimization of the immobilization conditions at any of these nanosupport interfaces involved controlling the enzyme interactions with the nanosupport or encapsulator (with or without a linker) (74) to preserve its functionality and catalytic behavior.…”

Section: Enzymes For Wastewater Treatmentmentioning

confidence: 99%

Emerging Enzyme-Based Technologies for Wastewater Treatment

Maloney

Dong

Campbell

et al. 2015

ACS Symposium Series

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In an effort to reduce the need for increased treatment and because of its high importance, interest in "green-based technologies" for wastewater management has picked up in recent years. Green methods aim to be logistically feasible, reliable, efficient, less time and energy consuming and highly cost-effective. This review provides an overview of the state-of-the-art technologies currently used for wastewater treatment and proposes developing novel solutions using enzymes and enzyme-based conjugates to remediate active chemicals and their metabolic products thereby ensuring water reusability. Addressing the global challenges of water quality with biotechnological approaches will provide the optimum conditions for prolonged green decontamination and reduced logistical burdens.

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“…Furthermore, the stability, under both storage and operational conditions, e.g., towards denaturation by heat or organic solvents, can be enhanced [7]. Currently, a range of supports have been reported for the immobilization of CPO, such as mesoporous supports [6,8,9], solgels [10,11], multi-walled carbon nanotubes [12,13] and other inorganic or organic solid supports [14,15]. The binding of an enzyme to a support (carrier) can be physical, ionic, or covalent in nature.…”

Section: Introductionmentioning

confidence: 99%