Regulating protein structure by Ligustrum robustum (Rxob.) Blume polyphenols during thermal processing: A potential...

Area of Science:

• Food Science
• Biochemistry
• Material Science

Background:

• Polyphenols are plant compounds with potential health benefits.
• Understanding their interaction with proteins is crucial for food processing.
• Ligustrum robustum (L. robustum) is a plant source of polyphenols.

Purpose of the Study:

• To investigate the effects of L. robustum polyphenols on myofibrillar protein (MP) and pea protein (PP) structures during thermal processing.
• To elucidate the underlying mechanisms of these interactions.
• To explore the application of these polyphenols in improving protein-based food quality.

Main Methods:

• Thermal analysis (Differential Scanning Calorimetry) to assess protein stability.
• Multispectral analysis (fluorescence quenching) to study polyphenol-protein interactions.
• Computational simulations to predict binding sites and interaction types.
• Texture analysis and microstructure observation of processed protein foods.

Main Results:

• Polyphenols enhanced the thermal stability of MP but reduced that of PP.
• Different polyphenol concentrations affected protein structures, reducing MP's random coils while increasing PP's.
• Polyphenols exhibited distinct binding affinities and interaction modes (hydrophobic vs. binding sites) with MP and PP.
• Incorporation of polyphenols improved the texture and microstructure of fried protein foods.

Conclusions:

• L. robustum polyphenols modulate MP and PP structures differently through specific molecular interactions during thermal processing.
• These findings provide a basis for utilizing L. robustum polyphenols to enhance the quality and safety of protein-rich food products.
• The study offers a novel perspective on controlling protein structure modifications in food applications.