Bovine alpha-lactalbumin assemblies with capsaicin: Formation, interactions, loading and physiochemical...

Area of Science:

• Food Science
• Biochemistry
• Materials Science

Background:

• Proteins and bioactives like capsaicin (CAP) offer health benefits but face delivery challenges.
• Effective delivery of CAP requires overcoming sensory, scientific, and technological hurdles.

Purpose of the Study:

• To investigate the complexation of CAP with native bovine alpha-lactalbumin (holo-ALA) and decalcified-ALA (apo-ALA).
• To explore the potential of ALA as an edible delivery vehicle for CAP.

Main Methods:

• Calorimetric and spectroscopic techniques were used to analyze ALA-CAP complexation.
• Isothermal Titration Calorimetry (ITC) determined binding stoichiometry and constants.
• Molecular docking simulated the binding interactions between CAP and ALA.

Main Results:

• ALA-CAP complexation is spontaneous, exothermic, and induces conformational changes in ALA.
• Hydrogen bonds drive CAP binding to holo-ALA, while hydrophobic interactions dominate apo-ALA binding.
• CAP-loaded colloids were formed with an encapsulation efficiency of 47.1%.

Conclusions:

• ALA shows potential as a carrier for CAP delivery.
• The study highlights the use of ALA-CAP interactions and controlled aggregation for developing functional food ingredients.