In this work, a Ni/Al hydrotalcite (HT) was used as glucose oxidase (GOx) immobilizer. Small-area and angle-resolved X-ray photoelectron spectra were recorded on HTs electrosynthesised on Pt in the absence and in the presence of GOx, and compared with those obtained for a Pt surface,modified with the electrosynthesized HT, on which a drop of GOx solution was deposited. The simultaneous electrodeposition of HT+GOx resulted in a compact deposit, thicker than the XPS sampling depth (>10 nm), that is not homogeneous in the lateral and indepth composition. The presence of GOx can be deduced comparing the N1s spectra of HT and HT + GOx: in the latter, the N1s component at 400 eV binding energy (BE) is predominant whilst, depending on the analyzed point, a small or no contribution from the component at 407.2 eV, due to nitrate, is revealed. Angle-resolved XPS provides evidence on the indepth composition of anions, cations and GOx. The results highlight the crucial role played by nickel in GOx immobilization. On the basis of the results, it can be suggested that enzyme activity is unevenly distributed and is localized in small areas, where Ni concentration is higher.
D. Addari, A. Mignani, E. Scavetta, D. Tonelli, A. Rossi (2011). An XPS investigation on glucose oxidase and Ni/Al Hydrotalcite interaction”. SURFACE AND INTERFACE ANALYSIS, 43, 816-822 [10.1002/sia.3636].
An XPS investigation on glucose oxidase and Ni/Al Hydrotalcite interaction”
MIGNANI, ADRIANA;SCAVETTA, ERIKA;TONELLI, DOMENICA;
2011
Abstract
In this work, a Ni/Al hydrotalcite (HT) was used as glucose oxidase (GOx) immobilizer. Small-area and angle-resolved X-ray photoelectron spectra were recorded on HTs electrosynthesised on Pt in the absence and in the presence of GOx, and compared with those obtained for a Pt surface,modified with the electrosynthesized HT, on which a drop of GOx solution was deposited. The simultaneous electrodeposition of HT+GOx resulted in a compact deposit, thicker than the XPS sampling depth (>10 nm), that is not homogeneous in the lateral and indepth composition. The presence of GOx can be deduced comparing the N1s spectra of HT and HT + GOx: in the latter, the N1s component at 400 eV binding energy (BE) is predominant whilst, depending on the analyzed point, a small or no contribution from the component at 407.2 eV, due to nitrate, is revealed. Angle-resolved XPS provides evidence on the indepth composition of anions, cations and GOx. The results highlight the crucial role played by nickel in GOx immobilization. On the basis of the results, it can be suggested that enzyme activity is unevenly distributed and is localized in small areas, where Ni concentration is higher.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.