Publication
Enzyme immobilization on Ag nanoparticles/polyaniline nanocomposites.
| Summary: | The performance of the modified electrodes toward urea hydrolysis was investigated via amperometric measurements, revealing a fast increase in cathodic current with a well-defined peak upon addition of urea to the electrolytic solution. The cathodic currents for the ITO/PAni/PVA–AgNP/urease electrodes were significantly higher than for the ITO/PAni/urease electrodes. The friendly environment provided by the ITO/PAni/PVA–AgNP electrode to the immobilized enzyme promoted efficient catalytic conversion of urea into ammonium and bicarbonate ions. Using the Michaelis–Menten kinetics equation, a KM app of 2.7mmolL−1 was obtained, indicating that the electrode architecture employedmay be advantageous for fabrication of enzymatic devices with improved biocatalytic properties. |
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| Main Authors: | Crespilho, Frank Nelson |
| Other Authors: | Iost, Rodrigo Michelin; Travain, Silmar Antonio; Oliveira Junior, Osvaldo Novais de; Zucolotto, Valtencir |
| Subject: | Silver nanocomposite Urease Polyaniline Enzyme immobilization Bioelectrochemistry |
| Year: | 2015 |
| Country: | Brazil |
| Document type: | article |
| Access type: | unknown |
| Associated institution: | IBICT |
| Language: | English |
| Origin: | Oasisbr |
| Summary: | The performance of the modified electrodes toward urea hydrolysis was investigated via amperometric measurements, revealing a fast increase in cathodic current with a well-defined peak upon addition of urea to the electrolytic solution. The cathodic currents for the ITO/PAni/PVA–AgNP/urease electrodes were significantly higher than for the ITO/PAni/urease electrodes. The friendly environment provided by the ITO/PAni/PVA–AgNP electrode to the immobilized enzyme promoted efficient catalytic conversion of urea into ammonium and bicarbonate ions. Using the Michaelis–Menten kinetics equation, a KM app of 2.7mmolL−1 was obtained, indicating that the electrode architecture employedmay be advantageous for fabrication of enzymatic devices with improved biocatalytic properties. |
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