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Related Concept Videos

Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Thermodynamics: Activity Coefficient01:24

Thermodynamics: Activity Coefficient

Activity is the measure of the effective concentration of the species in solution. It can be expressed as the product of the molar concentration of the species and its activity coefficient. The activity coefficient is a dimensionless quantity and depends on the total ionic strength of the solution.
The activity coefficient is a measure of the deviation from ideal behavior. When the ionic strength of the solution is minimal, the activity coefficient of an ionic species is close to unity, making...

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Related Experiment Video

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Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
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Assessing acetylcholinesterase activity at a polarizable liquid|liquid interface.

Salma Hafed-Khatiri1, Rayane-Ichrak Loughlani2, William Cheuquepan3

  • 1Instituto Universitario de Materiales de Alicante (IUMA), Universidad de Alicante, Carretera San Vicente s/n, Alicante, 03690, Spain.

Biosensors & Bioelectronics
|February 17, 2026
PubMed
Summary

This study demonstrates electrochemical monitoring of acetylcholinesterase (AChE) activity at a liquid|liquid interface. The method directly detects acetylcholine and choline, showing AChE functions in seawater and can be inhibited by malathion.

Keywords:
Acetylcholinesterase (AChE)Enzyme inhibition-based biosensorInterface between two immiscible electrolyte solutions (ITIES)Ion transferLiquid|liquid interfaceMalathion

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Area of Science:

  • Electrochemistry
  • Biochemistry
  • Analytical Chemistry

Background:

  • Acetylcholinesterase (AChE) is crucial for neurotransmission and a target for neurotoxins.
  • Monitoring AChE activity is vital for environmental and health assessments.
  • Existing methods for protein analysis at liquid|liquid interfaces (ITIES) often focus on adsorption or conformational changes.

Purpose of the Study:

  • To develop a novel electrochemical method for real-time monitoring of AChE activity at an ITIES.
  • To directly detect acetylcholine (ACh+) and choline (Ch+) without mediators.
  • To assess AChE activity and inhibition in complex matrices like synthetic seawater.

Main Methods:

  • Ion transfer voltammetry at a polarizable liquid|liquid interface (ITIES).
  • Direct electrochemical detection of ionic substrate (ACh+) and hydrolysis product (Ch+).
  • Enzyme inhibition studies using malathion.

Main Results:

  • Demonstrated direct, real-time electrochemical detection of ACh+ and Ch+ at the ITIES.
  • Confirmed AChE retains catalytic activity in Trizma buffer and synthetic seawater.
  • Quantified AChE inhibition by malathion, showing concentration-dependent effects.

Conclusions:

  • The ITIES is a versatile platform for studying enzyme kinetics and inhibition.
  • This electrochemical approach enables direct monitoring of enzymatic activity in complex environments.
  • The method holds potential for developing biosensors for neurotoxic pollutants.