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Area of Science:

  • Biotechnology
  • Biomaterials Science
  • Environmental Science

Background:

  • Enzyme immobilization on nanosurfaces is critical for biosensor development and biomaterial efficacy.
  • Chimeric proteins combining self-assembling hydrophobins with enzymes offer enhanced properties.
  • Arsenic contamination in water poses significant health risks, necessitating sensitive detection methods.

Purpose of the Study:

  • To create and characterize two chimeric proteins, ArsC-Vmh2 and Vmh2-ArsC, by fusing a hydrophobin (Vmh2) with an arsenate reductase (TtArsC).
  • To evaluate the enzymatic activity and immobilization capabilities of these chimeras on polystyrene and gold surfaces.
  • To assess their potential as electrochemical biosensors for arsenite (As(III)) detection.

Main Methods:

  • Heterologous expression of chimeric proteins in Escherichia coli and purification from inclusion bodies.
  • Enzymatic assays to determine arsenate reductase activity (As(V) to As(III) reduction).
  • Immobilization studies on polystyrene and gold electrodes, including reusability and stability assessments.
  • Electrochemical characterization using cyclic voltammetry and Langmuir isotherm modeling for As(III) recognition.

Main Results:

  • Chimeric proteins ArsC-Vmh2 and Vmh2-ArsC were successfully produced and purified.
  • Immobilized enzymes on polystyrene showed reusability up to three times with 50% activity loss after 15 days.
  • Immobilization on gold electrodes revealed Langmuir isotherm behavior for As(III) recognition, with high association constants (650-1200 L/mol).

Conclusions:

  • Gold-immobilized ArsC-Vmh2 and Vmh2-ArsC function effectively as electrochemical biosensors for As(III) detection.
  • The chimeric proteins exhibit favorable immobilization properties and enzyme stability.
  • These findings highlight the potential of engineered enzymes for sensitive and reliable arsenic monitoring in environmental and biological samples.