Modulation of sunflower seed protein structure and functionality by chlorogenic acid interaction and stepwise...

Area of Science:

• Food Science
• Protein Chemistry
• Plant-based Ingredients

Background:

• Sunflower seed protein is a valuable plant-based protein source.
• Chlorogenic acid (CGA) in sunflower meal causes undesirable browning and off-flavors, limiting its use in food products.

Purpose of the Study:

• To investigate the interaction mechanisms between CGA and sunflower seed protein.
• To evaluate the impact of CGA removal on protein structure, functionality, and sensory attributes.

Main Methods:

• Systematic investigation of CGA-protein interactions.
• Dephenolization techniques to remove CGA from sunflower meal.
• Analysis of protein structural integrity, functional properties (emulsion, gelling, foaming), and sensory profile.

Main Results:

• Moderate dephenolization (>92% CGA removal) improved protein structural compactness, indicated by increased β-sheet content and fluorescence.
• Excessive CGA binding negatively affected gelling and foaming properties.
• Moderate CGA removal enhanced emulsion stability to approximately 80% and maintained oil-holding capacity.
• CGA binding caused discoloration and, upon oxidation, generated off-flavors through aldehydes and ketones.
• Moderately dephenolized protein exhibited pleasant fruity notes.

Conclusions:

• Moderate removal of CGA significantly enhances the structural integrity, functional performance, and sensory profile of sunflower seed protein.
• This study provides a theoretical foundation for the expanded application of sunflower seed protein in the food industry.