Insights into the interactions between etheric compounds and myofibrillar proteins using multi-spectroscopy,...

Area of Science:

• Food Science
• Protein Chemistry
• Molecular Dynamics

Background:

• Myofibrillar proteins (MP) are crucial in food systems.
• Understanding interactions with additives like etheric compounds (EC) is important for texture and flavor.
• Protein conformational changes influence functional properties.

Purpose of the Study:

• To investigate the impact of etheric compounds (EC) on myofibrillar protein (MP) characteristics.
• To elucidate the interaction mechanisms between EC and MP.
• To assess the effect of EC on protein unfolding, aggregation, and flavor compound interactions.

Main Methods:

• Fourier transform infrared spectroscopy (FTIR) to analyze protein structure.
• Zeta potential measurements to assess surface charge.
• Rheological analysis to evaluate gel network properties.
• Molecular dynamics simulations to model molecular interactions.

Main Results:

• EC formed complexes with MP via hydrogen bonding, increasing alpha-helix and decreasing beta-sheet content.
• MP unfolding led to larger aggregates, enhanced negative surface charge (lower zeta potential), and a less rigid gel structure.
• EC enhanced the release of aldehyde compounds.
• Anethole (an EC) reduced myosin-decanal binding affinity by disrupting hydrogen bonds and hydrophobic contacts.

Conclusions:

• Etheric compounds significantly alter myofibrillar protein structure and function.
• These modifications influence protein aggregation, charge, and the release of flavor compounds.
• Findings provide a basis for controlling protein-flavor interactions in food products.