Deciphering the Stevioside-Whey Protein Binding Mechanism: A Synergistic Multispectral and Computational Docking...

Area of Science:

• Food Science
• Biochemistry
• Molecular Biophysics

Background:

• Stevioside (STE) and whey protein (WP) are common food ingredients.
• Understanding their interaction is key for developing functional foods.

Purpose of the Study:

• To elucidate the molecular mechanisms of stevioside-whey protein complexation.
• To establish a structure-energy framework for STE-WP interactions.

Main Methods:

• Multispectral characterization (UV-Vis absorption, fluorescence spectroscopy).
• Thermodynamic analysis (calculating ΔS, ΔH, ΔG).
• Circular dichroism spectroscopy for secondary structure analysis.
• Computational modeling (molecular docking, molecular dynamics simulations).

Main Results:

• STE-WP complex formation confirmed via static quenching.
• Binding is an entropy-driven process (ΔS = +976.7 J·mol⁻¹·K⁻¹).
• STE binding significantly increased α-helix content (16% to 40.5%) in WP.
• Molecular simulations showed STE localizes in WP's hydrophobic pockets, stabilized by H-bonds and hydrophobic interactions.

Conclusions:

• The study provides a comprehensive understanding of STE-WP complexation mechanisms.
• Findings offer a theoretical basis for optimizing STE-WP applications in functional foods.
• The established framework aids in designing food products with enhanced properties.