AI Article Synopsis
- The study investigates the formation of complexes between ovalbumin nanoparticles (OVAn) and linoleic acid (LA), focusing on their stoichiometric, kinetic, and thermodynamic properties.
- It was found that about 49 LA molecules bind to each OVA monomer with a binding constant of roughly 9.80×10(5) M, indicating a strong interaction.
- The adsorption of LA on OVAn occurs rapidly within an hour and is characterized as a spontaneous, endothermic process driven by entropy, with size measurements showing both OVAn and LA-OVAn complexes are under 100 nm.
Article Abstract
Stoichiometric, kinetic and thermodynamic aspects of complex formation between heat-induced aggregates of ovalbumin (ovalbumin nanoparticles, OVAn) and linoleic acid (LA) were evaluated. Extrinsic fluorescence data were fitted to modified Scatchard model yielding the following results: n: 49±2 LA molecules bound per OVA monomer unit and Ka: 9.80±2.53×10(5)M. Kinetic and thermodynamic properties were analyzed by turbidity measurements at different LA/OVA monomer molar ratios (21.5-172) and temperatures (20-40°C). An adsorption approach was used and a pseudo-second-order kinetics was found for LA-OVAn complex formation. This adsorption process took place within 1h. Thermodynamic parameters indicated that LA adsorption on OVAn was a spontaneous, endothermic and entropically-driven process, highlighting the hydrophobic nature of the LA and OVAn interaction. Finally, Atomic Force Microscopy imaging revealed that both OVAn and LA-OVAn complexes have a roughly rounded form with size lower than 100nm.
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| http://dx.doi.org/10.1016/j.foodchem.2016.05.137 | DOI Listing |
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