Exploring the interaction between myofibrillar proteins and pyrazine compounds: Based on molecular docking, molecular...

Area of Science:

• Food Science
• Protein Chemistry
• Sensory Science

Background:

• Consumer preference for processed meats heavily relies on flavor.
• Myofibrillar proteins (MPs) interact with flavor compounds, influencing the final taste.
• Understanding these interactions is key to improving processed meat quality.

Purpose of the Study:

• To investigate how heating affects the interaction between myofibrillar proteins (MPs) and pyrazine flavor compounds.
• To elucidate the underlying mechanisms of these interactions.
• To provide insights for enhancing the flavor of processed meats.

Main Methods:

• Multispectral analysis to study protein structural changes.
• Molecular docking and molecular dynamics simulations to analyze protein-flavor interactions.
• Quantification of surface hydrophobicity, sulfhydryl (SH) content, and zeta potential.

Main Results:

• Heating caused structural reconstruction and expansion of MPs, altering hydrophobicity and SH content.
• A decrease in MPs' zeta potential was observed with short heating times.
• Positive correlation between beta-sheet content and pyrazine adsorption capacity.
• Molecular docking identified 13 binding sites and four interaction forces (van der Waals, C-H bonds, alkyl, π-alkyl).

Conclusions:

• Optimized heat treatment enhances the binding capacity of MPs to pyrazine flavor compounds by exposing more binding sites.
• Structural modifications in MPs during processing significantly impact their ability to bind flavor substances.
• This research offers a pathway to improve processed meat flavor and encourage consumption through controlled processing.