High pressure-low temperature processing of food proteins

Area of Science:

• Food Science
• Protein Chemistry
• Food Processing

Background:

• High pressure-low temperature (HP-LT) processing offers
• cold
• pasteurization and mitigates freezing damage to food structures.
• Conventional freezing at 0.1 MPa produces large ice crystals, whereas fast pressure release freezing yields smaller ice nuclei.

Purpose of the Study:

• Investigate HP-LT effects on protein unfolding, dissociation, and aggregation.
• Minimize or control structural changes and aggregation reactions in food proteins.
• Enhance protein functional properties through HP-LT treatment.

Main Methods:

• Studied HP-LT effects on beta-lactoglobulin and casein micelles.
• Applied pressures up to 300 MPa at low/sub-zero temperatures, with analysis after pressure release.
• Utilized UV spectroscopy under pressure (up to 200 MPa) to monitor reversible structural changes.

Main Results:

• HP-LT processing up to 300 MPa at low/sub-zero temperatures minimized aggregation in beta-lactoglobulin solutions.
• Low-temperature treatments enhanced the size reduction of casein micelles.
• HP-LT processing influences protein structure and aggregation behavior.

Conclusions:

• HP-LT processing is effective in minimizing aggregation reactions in whey proteins like beta-lactoglobulin.
• This method promotes casein micelle size reduction, suggesting potential for improved food texture and stability.
• HP-LT processing presents a promising approach for modifying protein functionality and structure in food applications.