Journal
BIOSENSORS-BASEL
Volume 12, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/bios12110939
Keywords
sulfonated starch; polyaniline; graphene; electrical nanocomposite; tyrosinase
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The interaction between tyrosinase and sulfonated starch-graft-polyaniline@graphene nanocomposite was investigated using electrochemical methods. The immobilized tyrosinase showed activity in the electrochemical detection of three substrates. The nanocomposite was characterized and the enzyme immobilization was successfully achieved through a drop-casting technique. The modified electrode exhibited enhanced catalytic effects on the redox agent compared to the bare electrode.
The interaction of tyrosinase with sulfonated starch-graft-polyaniline@graphene (SSt-g-PANI@G) nanocomposite was investigated by electrochemical methods. The activity of the immobilized tyrosinase (Tyase) was proved by the electrochemical detection of three substrates (L-dopa, caffeic acid, and catechol). The SSt-g-PANI@G nanocomposite was characterized by Fourier-transform infrared spectra (FT-IR), X-ray diffraction (XRD), field emission scanning electron microscopy (FESEM), energy-dispersive X-ray analysis (EDX), and thermogravimetric analysis (TGA). To immobilize tyrosinase on the surface of the nanocomposite, a simple drop-casting technique was used. The presence of sulfuric acid and hydroxyl groups in SSt, amine groups in PANI, and high surface-to-volume ratio and electrical conductivity of graphene in the prepared nanocomposite led to good enzyme immobilization on the electrode surface. The modified electrode showed a suitable catalytic effect on the electrochemical redox agent, compared with the bare electrode. The peak current responses for three substrates were studied with a calibration curve derived using cyclic voltammetry (CV) and differential pulse voltammetry (DPV). In addition, the fabricated SSt-g-PANI@G/Tyase/GCE showed a more suitable response to catechol, L-dopa, and caffeic acid substrates, respectively.
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