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Exploring the electrochemical behaviour of digestive enzymes at a liquid|liquid micro-interface array.
Shaheda Zannah1, Damien W M Arrigan1
1School of Molecular and Life Sciences, Curtin University, GPO Box U1987, Perth, Western Australia 6845, Australia.
Bioelectrochemistry (Amsterdam, Netherlands)
|February 9, 2025
Summary
Electrochemical methods at liquid/liquid micro-interfaces enable sensitive detection of the digestive enzymes trypsin and pepsin. Stripping voltammetry significantly improves detection limits for these important biomolecules.
Area of Science:
- Analytical Chemistry
- Electrochemistry
- Biochemistry
Background:
- Trypsin and pepsin are key digestive enzymes crucial for protein breakdown.
- Understanding their electrochemical behavior is vital for developing new detection methods.
- Liquid/liquid (L|L) micro-interfaces offer unique platforms for studying biomacromolecules.
Purpose of the Study:
- To investigate the electrochemical behavior and detection of trypsin and pepsin.
- To evaluate the efficacy of liquid/liquid (L|L) micro-interface arrays for protein analysis.
- To compare the electrochemical characteristics of trypsin and pepsin.
Main Methods:
- Utilized cyclic voltammetry (CV) and adsorption stripping voltammetry (AdSV).
- Employed a liquid/liquid (L|L) micro-interface array setup.
- Investigated protein electroactivity in 10 mM hydrochloric acid.
- Assessed protein impact on ion transfer using tetrapropylammonium ion (TPrA+).
Main Results:
- Both trypsin and pepsin were electroactive in 10 mM HCl.
- AdSV enabled sub-micromolar detection, surpassing CV's 30 μM limit.
- Pepsin exhibited ill-defined electrochemical behavior and significantly impeded ion transfer.
- Trypsin showed minimal impedance to ion transfer, indicating distinct properties.
Conclusions:
- Electrochemical analysis at L|L micro-interfaces is a viable tool for studying biomacromolecules.
- Adsorption stripping voltammetry offers enhanced sensitivity for trypsin and pepsin detection.
- Distinct electrochemical behaviors of trypsin and pepsin were observed, highlighting their differences.
