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Updated: Feb 2, 2026

Measurement of Particle Size Distribution in Turbid Solutions by Dynamic Light Scattering Microscopy

Measurement of Particle Size Distribution in Turbid Solutions by Dynamic Light Scattering Microscopy

Published on: January 9, 2017

Aldolase Does Not Show Enhanced Diffusion in Dynamic Light Scattering Experiments.

Yifei Zhang¹, Megan J Armstrong¹, Neda M Bassir Kazeruni¹

¹Department of Biomedical Engineering , Columbia University , 351L Engineering Terrace, 1210 Amsterdam Avenue , New York , New York 10027 , United States.

|November 29, 2018

Summary

This summary is machine-generated.

Enzymes do not show enhanced diffusion during catalysis. Dynamic Light Scattering (DLS) found no significant change in aldolase diffusion, challenging previous Fluorescence Correlation Spectroscopy (FCS) findings.

Keywords:

DLS catalysis enhanced diffusion enzymes nanomotors

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Area of Science:

Biophysics
Enzymology

Background:

Recent studies suggest enzymes exhibit increased diffusion when catalytically active, a phenomenon supported by some theories.
However, other theoretical work and potential artifacts in Fluorescence Correlation Spectroscopy (FCS) measurements question these findings.

Purpose of the Study:

To investigate the diffusion coefficient of aldolase in its active and inactive states using Dynamic Light Scattering (DLS).
To address the discrepancy between experimental observations of enhanced enzyme diffusion and theoretical challenges.

Main Methods:

Utilized Dynamic Light Scattering (DLS) to measure the diffusion coefficient of the enzyme aldolase.
Compared diffusion coefficients in the absence and presence of a saturating substrate concentration.

Main Results:

DLS measurements demonstrated an experimental error of 3%.
No statistically significant change in the aldolase diffusion coefficient was observed, even with a saturating substrate concentration.

Conclusions:

The findings support the possibility of photophysical artifacts influencing previous FCS measurements.
This study challenges the hypothesis that enzyme catalytic activity can lead to self-propulsion and enhanced diffusion.