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Enzyme Kinetics

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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.
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Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...

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Related Experiment Video

Updated: Jun 12, 2026

Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation

Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation

Published on: August 28, 2017

Coupled enzyme reactions in multicompartment microparticles.

Hans Bäumler¹, Radostina Georgieva

¹Berlin-Brandenburg Center of Regenerative Therapies, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany. hans.baeumler@charite.de

Biomacromolecules

|May 22, 2010

Summary

Researchers developed reusable spherical biopolymer particles encapsulating enzymes like horseradish peroxidase (HRP) and glucose oxidase (GOX). These multicompartment particles allow precise enzyme placement, enabling visualization of reaction kinetics at the microscale.

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Aqueous Droplets Used as Enzymatic Microreactors and Their Electromagnetic Actuation

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Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Published on: January 26, 2024

Area of Science:

Biomaterials Science
Enzyme Engineering
Nanotechnology

Background:

Enzyme immobilization is crucial for biocatalysis and biosensing.
Controlling enzyme localization within microstructures is challenging.
Developing reusable and precisely organized enzyme carriers is a key goal.

Purpose of the Study:

To fabricate reusable, multicompartment spherical biopolymer particles for controlled enzyme encapsulation.
To investigate the impact of enzyme spacing on coupled reaction kinetics within individual microparticles.
To visualize and analyze enzyme reaction dynamics at the microscale.

Main Methods:

Spherical biopolymer particles fabricated via coprecipitation with calcium carbonate, followed by cross-linking and support dissolution.
Enzyme loading (horseradish peroxidase (HRP), glucose oxidase (GOX), beta-glucosidase (beta-Glu)) into distinct compartments.
Confocal laser scanning microscopy used to visualize reaction progression with fluorogenic substrates.
Varying spacing between enzyme compartments using bovine serum albumin (BSA).

Main Results:

Successfully created reusable enzyme-loaded particles with 30-50% initial activity after six uses.
Demonstrated stepwise incorporation and precise spatial arrangement of three coupled enzymes in concentric compartments.
Observed significant influence of spacing on reaction kinetics, indicating diffusion limitations of intermediates.
Visualized enzyme reaction initiation and termination within single microparticles.

Conclusions:

Multicompartment biopolymer particles offer a platform for precise enzyme organization and study of reaction kinetics.
Spatial arrangement and spacing significantly impact the efficiency of coupled enzymatic reactions.
This microscale approach provides unprecedented insights into enzyme-substrate interactions within engineered microenvironments.