Pulsed electric field modulates lactoferrin conformation to enhance quercetin binding and complex stability

Area of Science:

• Food Science
• Biotechnology
• Materials Science

Background:

• Quercetin (QUE) has limited use due to poor solubility and bioavailability.
• Lactoferrin (LF) is a potential carrier but its structure hinders efficient binding of hydrophobic compounds like QUE.

Purpose of the Study:

• To investigate the use of pulsed electric field (PEF) to modulate LF structure for enhanced QUE delivery.
• To optimize LF-QUE complex formation for improved stability and bioavailability.

Main Methods:

• Continuous-flow pulsed electric field (PEF) treatment applied to lactoferrin (LF).
• Characterization of LF-QUE complexes using multispectral analysis and molecular simulations.
• Assessment of QUE loading capacity, binding affinity, colloidal dispersibility, thermal stability, and in vitro bioaccessibility.

Main Results:

• Moderate PEF (10 kV·cm⁻¹) induced controlled LF unfolding, increasing QUE loading by 40.2%.
• Excessive PEF (≥15 kV·cm⁻¹) caused cross-linking, reducing loading efficiency.
• The LF10-QUE20 complex showed enhanced binding affinity, stability (86.3°C), and a 21.5% increase in QUE bioaccessibility.
• PEF facilitated a crystalline-to-amorphous transition of QUE and improved binding stability through various molecular interactions.

Conclusions:

• PEF is a facile, non-thermal method to optimize LF as a delivery system for hydrophobic bioactives.
• This approach enhances the loading, stability, and bioavailability of QUE for functional food applications.
• PEF offers an alternative to conventional methods, avoiding denaturation and chemical residues.