Kinetic Analysis of Enzyme-Catalyzed Reactions Using Electrochemical Impedance Spectroscopy

DOI 10.66715/jsccr/2025.v2.i1.017 Original Research | 2025 | Volume 2 | Issue 1 | Page 1-07

1. Dr. Amit Thakur, Aadharshila Academy, Jogindernagar, Distt Mandi, Himachal Pradesh 175015

2. Mrs Sarita Kumari, PGT Chemistry, Govt Sen Sec School Barot, Distt Mandi Himachal Pradesh 175015

3. Mr Arvind Thakur, Senior Research Analyst at Abryl Laboratories Dera Bassi 140507

Kinetic Analysis of Enzyme-Catalysed Reactions Using Electrochemical Impedance Spectroscop.

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Corresponding Author:-

Dr. Amit Thakur,

Aadharshila Academy,

Jogindernagar, Distt Mandi,

Himachal Pradesh 175015

Abstract

Enzyme-catalysed reactions play a fundamental role in biological systems, pharmaceutical research, clinical diagnostics, and industrial biotechnology. Accurate determination of enzyme kinetics is essential for understanding catalytic efficiency, substrate affinity, and reaction mechanisms. Electrochemical Impedance Spectroscopy (EIS) has emerged as a powerful, non-destructive, and highly sensitive analytical technique for monitoring enzyme-mediated reactions in real time. This study investigates the application of EIS for the kinetic analysis of enzyme-catalysed reactions by evaluating changes in charge transfer resistance, double-layer capacitance, and impedance spectra during enzymatic substrate conversion. Enzyme-modified electrodes were employed to facilitate selective biocatalytic reactions, and impedance measurements were recorded across a broad frequency range under varying substrate concentrations. The obtained impedance parameters were correlated with classical Michaelis–Menten kinetic models to determine kinetic constants, including maximum reaction velocity (Vmax) and Michaelis constant (Km). Results demonstrated a strong relationship between impedance responses and enzymatic activity, enabling precise characterization of reaction rates and substrate-enzyme interactions. The EIS-based approach provided enhanced sensitivity, rapid data acquisition, and reduced reagent consumption compared with conventional spectrophotometric methods. Furthermore, the technique allowed continuous monitoring of reaction progression without disrupting the biochemical system. The findings highlight the potential of electrochemical impedance spectroscopy as a versatile tool for enzyme kinetic studies, biosensor development, and biomedical diagnostics. This methodology offers significant advantages for real-time biochemical analysis and supports the advancement of electrochemical platforms for investigating complex enzymatic processes in research and industrial applications.