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Related Experiment Video

Updated: Jun 21, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Published on: April 28, 2022

Structural changes in confined lysozyme.

Eduardo Reátegui¹, Alptekin Aksan

¹Department of Mechanical Engineering, Biostabilization Laboratory, University of Minnesota, Minneapolis, MN, USA.

Journal of Biomechanical Engineering

|July 31, 2009

Summary

Encapsulating proteins in nanoporous gels enhances stability. Confined lysozyme showed increased structure at cold temperatures but lower heat denaturation temperatures, influenced by solvent dynamics and pore size.

Area of Science:

Biomaterials Science
Protein Chemistry
Spectroscopy

Background:

Proteins and enzymes encapsulated in nanoporous gels offer potential for biosensing, biocatalysis, and biosynthesis.
Encapsulation can enhance macromolecule activity, functionality, and resistance to extreme pH and temperature conditions.

Purpose of the Study:

To investigate the structural transitions of encapsulated lysozyme across a wide temperature range (-120°C to 100°C).
To compare the thermal stability of encapsulated lysozyme with lysozyme in solution.

Main Methods:

Intrinsic fluorescence spectroscopy was used to monitor protein structure.
Fourier transform infrared spectroscopy (FTIR) provided insights into molecular vibrations and structural changes.
Lysozyme was encapsulated within a nanoporous gel matrix.

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Main Results:

Encapsulated lysozyme exhibited increased structural order at cryogenic temperatures, with no cold denaturation observed.
A decrease of 15°C in the onset of heat denaturation was observed for encapsulated lysozyme compared to free lysozyme.
Altered solvent dynamics and pore size distribution within the nanoporous gel influenced denaturation behavior.

Conclusions:

Nanoporous gel encapsulation significantly alters the thermal denaturation profile of lysozyme.
The confinement effects, including solvent dynamics and pore characteristics, are critical factors in protein stability.
This study provides valuable insights for designing protein-based nanomaterials with tailored stability for various applications.