Potential unlocking of self-assembled phosphorylated ovalbumin in stabilizing linalool nanoemulsion: Structural, interfacial, and sustained-release properties

This study explored the role of self-assembled phosphorylated ovalbumin (SPOVA) in stabilizing linalool nanoemulsion (LLN) through pH-controlled and heat-induced phosphorylation. Fluorescence spectroscopy and Fourier Transform Infrared spectroscopy indicated that hydrophobic interactions, electrostatic interactions, and hydrogen bonding drove the self-assembly of SPOVA, while further molecular docking revealed strong binding between ovalbumin (OVA) and sodium tripolyphosphate (STPP). The colloidal characteristics of SPOVA dispersed in aqueous solutions were examined by zeta potential and turbidity analysis. SPOVA samples exhibited lower interfacial tension under alkaline conditions, particularly SPOVA9, which presented the highest interfacial adsorption rate and an oil-water contact angle close to 90 degrees, indicative of amphiphilic properties necessary for effectively stabilizing emulsions. Compared to non-phosphorylated OVA (NOVA), SPOVA9-stabilized LLN (LLNSPOVA9) showed superior stability, with excellent sustained-release behavior over 60 days. TEM revealed densely packed amyloid-like fibrils at the oil-water interface for LLN-SPOVA9, which can significantly enhance the interfacial stability. This study highlights the potential of SPOVA9 as a novel stabilizer for encapsulating aromatic compounds with nanoemulsions, providing insights into flavor encapsulation.