Mechanistic understanding of the effects of ovalbumin-nanoliposome interactions on ovalbumin emulsifying properties
Qian Wang, Min‐Hsiung Pan, Yi‐Shiou Chiou, Zhenshun Li, Shudong Wei, Xiaoli Yin, Baomiao Ding
Abstract
The effects of ovalbumin (OVA) and nanoliposome interactions on ovalbumin emulsifying properties were researched by UV–vis absorption, fluorescence, circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR), particle size, Zeta-potential, surface hydrophobicity, contact angle (θ) and free sulfydryl (SH) content. Fluorescence analysis showed that the fluorescences of OVA were quenched after complexation with nanoliposomes. The secondary structure of OVA was slightly altered after the interactions. The peak shifts of C–H stretching vibration and O–H stretching vibration were observed in OVA-NL FTIR spectrum. It could be speculated that the hydrogen bonds and hydrophobic forces played a vital role in the interaction between OVA and NL. The interfacial tension of OVA was significantly decreased, and the surface hydrophobicity, θ and the content of free SH content of OVA increased in the presence of nanoliposomes. Furthermore, EAIs and ESIs of OVA increased from 32.55 to 64.79 m2/g, and from 30.23 to 95.48 min with the nanoliposome concentration increasing, respectively. These results showed that the vesicles could interact with OVA via non-covalent forces, and the emulsifying properties of OVA could be obviously improved after interaction with nanoliposomes. Our work provided a new insight into the application of OVA-NL in food industry.