Magnesium Ion-Regulated Aggregation Mechanism of Zein-Ovalbumin Complexes
Min Huang1,2, Yuanru Xu1, Hao Li1
1School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China.
The Journal of Physical Chemistry. B
|February 25, 2026
Summary
Magnesium ions (Mg2+) modulate protein aggregation during food processing. Mg2+ inhibited Zein and Zein-Ovalbumin aggregation but enhanced Ovalbumin aggregation, offering insights into food structure stabilization.
Area of Science:
- Food Science
- Biochemistry
- Materials Science
Background:
- Metal ions significantly impact protein aggregation during food processing.
- Understanding these interactions is key to enhancing food structure and stability.
- Investigating magnesium ions (Mg2+) provides insights into protein behavior.
Purpose of the Study:
- To investigate the effect of Mg2+ on the aggregation kinetics of Zein, Ovalbumin, and their complexes under thermal treatment.
- To correlate protein conformational changes with aggregation behavior using theoretical and experimental approaches.
- To elucidate the role of Mg2+ in modulating protein-protein interactions and thermal stability.
Main Methods:
- Aggregation kinetic modeling to analyze protein aggregation.
- Fourier transform infrared spectroscopy (FTIR) to assess protein structure.
- Molecular dynamics (MD) simulations to investigate binding free energy and interactions.
- Analysis of hydrophobic and free sulfhydryl (-SH) group exposure.
Main Results:
- Mg2+ inhibited the aggregation of Zein and Zein-Ovalbumin complexes but enhanced Ovalbumin aggregation.
- Conformational changes, including alterations in hydrophobic and -SH group exposure, were linked to aggregation modulation.
- Thermal stability of protein complexes increased due to electrostatic and hydrogen-bonding interactions, further stabilized by Mg2+.
- Mg2+ reduced binding free energy within Zein-Ovalbumin complexes via electrostatic shielding.
Conclusions:
- Mg2+ plays a critical role in regulating protein aggregation behavior in complex food systems.
- The findings offer mechanistic insights for using metal ions to control protein structure and function.
- This research supports the strategic application of Mg2+ for optimizing the properties of complex protein ingredients.
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