Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 23, Issue 20, Pages -Publisher
MDPI
DOI: 10.3390/ijms232012569
Keywords
tyrosinase; laccase; screen-printed electrode; single-walled carbon nanotube; oleuropein; olive oil
Funding
- Romanian Ministry of Education and Research, CNCS-UEFISCDI [PN-III-P4-ID-PCE-2020-0923]
Ask authors/readers for more resources
This study achieved qualitative and quantitative determination of oleuropein in commercial EVOO samples using electrochemical techniques. Enzyme biosensors were constructed with successful immobilization of enzymes on carbon nanotube-modified electrodes, demonstrating efficient detection of oleuropein. The tyrosinase-based biosensor showed superior sensitivity towards oleuropein compared to the laccase-based one.
Oleuropein (OLEU) is an important indicator of the quality and authenticity of extra virgin olive oils (EVOO). Electrochemical sensors and biosensors for the detection of oleuropein can be used to test the adulteration of extra virgin olive oils. The present study aimed at the qualitative and quantitative determination of oleuropein in commercial EVOO samples by applying electrochemical techniques, cyclic voltammetry (CV) and square wave voltammetry (SWV). The sensing devices used were two newly constructed enzyme biosensors, supported on single-layer carbon-nanotube-modified carbon screen-printed electrode (SPE/SWCNT) on whose surface tyrosinase (SPE/SWCNT/Tyr) and laccase (SPE/SWCNT/Lac) were immobilized, respectively. The active surfaces of the two biosensors were analyzed and characterized by different methods, cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS) and Fourier transform infrared spectroscopy (FTIR) and the results confirmed the efficient immobilization of the enzymes. SPE/SWCNT/Tyr was characterized by a low detection limit (LOD = 9.53 x 10(-8) M) and a very good sensitivity (0.0718 mu A center dot mu M-1 center dot cm(-2)) over a wide linearity range from 0.49 to 11.22 mu M. The process occurring at the biosensor surface corresponds to kinetics (h = 0.90), and tyrosinase showed a high affinity towards OLEU. The tyrosinase-based biosensor was shown to have superior sensitive properties to the laccase-based one. Quantitative determination of OLEU in EVOOs was performed using SPE/SWCNT/Tyr and the results confirmed the presence of the compound in close amounts in the EVOOs analysed, proving that they have very good sensory properties.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available