Molecular interaction between myofibrillar protein and beta-carotene during heating

Area of Science:

• Food Science
• Biophysics
• Biochemistry

Background:

• Beta-carotene (β-C) is a beneficial phytochemical with poor intestinal absorption due to hydrophobicity and instability.
• Myofibrillar protein (MP) systems offer a potential solution for enhancing β-C bioavailability.
• Temperature is a critical factor influencing the efficacy of MP-based delivery systems.

Purpose of the Study:

• To investigate the effect of temperature on the interaction between beta-carotene (β-C) and myofibrillar proteins (MP).
• To understand how temperature influences the binding mechanisms and structural changes relevant to β-C delivery.

Main Methods:

• Multispectral analysis to probe molecular changes.
• Surface Plasmon Resonance (SPR) to quantify binding kinetics and affinity.
• Molecular dynamics simulations to visualize and analyze intermolecular interactions at the molecular level.

Main Results:

• The primary interaction force between β-C and MP transitioned from Van der Waals to hydrophobic interactions around 37°C.
• Observed changes in protein spatial structure and molecular thermal motion correlate with the shift in interaction forces.
• This temperature-dependent interaction modulation is key to optimizing β-C encapsulation within MP structures.

Conclusions:

• Selecting an optimal temperature, particularly near 37°C, is crucial for designing effective heat-induced MP transport systems for beta-carotene.
• Understanding temperature-mediated molecular interactions enhances the development of improved nutraceutical delivery systems.
• This research provides insights into tailoring protein-based delivery systems for hydrophobic compounds like β-C.