Related Experiment Video
Updated: Oct 23, 2025
Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
Published on: June 29, 2021
Aggregation and deaggregation: The effect of high-pressure homogenization cycles on myofibrillar proteins aqueous
Chang Su1, Zhifei He2, Zefu Wang1
1College of Food Science, Southwest University, No. 2 Tiansheng Road, Beibei District, Chongqing 400715, China.
Abstract:
Myofibrillar proteins (MPs) have not been fully used for a long time due to its poor solubility in low ionic strength solutions. The study explored the effect of high pressure homogenization (HPH) cycles under two pressures on the solubility of MPs. The MPs solubility increased with HPH cycles (p < 0.05), the results of turbidity, appearance, droplet size indicated that the increase of solubility was due to MPs depolymerization, excessive HPH cycles (25k psi for 11 cycles) would lead to protein re-aggregation but does not affect solubility (p>0.05). SDS-PAGE suggested that myosin formed soluble polymers with different molecular weights through disulfide bonds during HPH cycles, the polymer consisted of myosin subunits of different molecular weights. Endogenous fluorescence spectra, intermolecular chemical forces, isoelectric point analysis and free amino acids (FAAs) indicated that the dissolution of polymers in low ionic strength media was dominated by polar environment and intermolecular steric hindrance, but not to FAAs.
Insights
High pressure homogenization improves myofibrillar protein (MP) solubility by breaking down protein structures. While excessive cycles can cause re-aggregation, solubility remains enhanced, driven by steric hindrance and polar environments.
Area of Science:
- Food Science and Technology
- Protein Chemistry
- Biophysical Chemistry
Background:
- Myofibrillar proteins (MPs) exhibit poor solubility in low ionic strength solutions, limiting their application.
- Understanding protein behavior under processing conditions is crucial for optimizing food ingredient functionality.
Purpose of the Study:
- To investigate the impact of high pressure homogenization (HPH) cycles on the solubility of myofibrillar proteins.
- To elucidate the mechanisms underlying HPH-induced changes in MP solubility and structure.
Main Methods:
- Application of high pressure homogenization (HPH) at varying pressures and cycle counts.
- Assessment of protein solubility using turbidity, appearance, and droplet size analysis.
- Structural analysis via SDS-PAGE, endogenous fluorescence spectra, intermolecular chemical force measurements, isoelectric point determination, and free amino acid (FAA) analysis.
Main Results:
- MP solubility significantly increased with HPH cycles (p < 0.05), attributed to protein depolymerization.
- Excessive HPH cycles (e.g., 25k psi for 11 cycles) led to protein re-aggregation but did not negate the solubility enhancement (p > 0.05).
- SDS-PAGE revealed myosin forming soluble polymers via disulfide bonds, composed of subunits with varying molecular weights.
Conclusions:
- High pressure homogenization is an effective method to enhance myofibrillar protein solubility.
- The improved solubility in low ionic strength media is primarily governed by polar environment and intermolecular steric hindrance, not free amino acids.
- HPH-induced depolymerization and subsequent polymer formation offer a pathway to overcome solubility limitations of MPs.
More Related Videos
08:48High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
08:24Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
Published on: August 18, 2017
Related Concept Videos
01:32Tissue Homogenization and Cell Lysis
Mechanical methods of tissue homogenization
These methods rely on applying external physical force to disrupt...
03:00Molecular Chaperones and Protein Folding
The...
01:22Protein Folding