期刊
FOOD HYDROCOLLOIDS
卷 132, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2022.107876
关键词
Protein-protein interaction; Complex nanoparticle; Molecular dynamics simulation; Surface morphology; Fourier transform infrared spectroscopy
资金
- Natural Science Foundation of Zhejiang Province [LGN21C200012]
- National Natural Science Foundation of China [21203166]
- Open Project of State Key Laboratory of Physical Chemistry of Solid Surface of Xiamen University [202007]
- Professional Development Project for Domestic Visiting Scholars and Teachers in Colleges and Universities in Zhejiang Province [FX2020017]
The interaction mechanism between zein and lysozyme was investigated in this study. The results showed that zein-lysozyme complex nanoparticles were stable at a ratio of 2:1 and pH 4.0, with electrostatic and hydrophobic interactions being the main driving forces. Hydrogen bonding also played a role, but not as significant. The molecular dynamics simulations revealed that lysozyme preferred to bind to the protruding area of zein, and certain residues in both zein and lysozyme contributed significantly to the binding. These findings provide scientific guidance for the potential application of zein-lysozyme nanoparticles in the food industry as delivery systems or emulsion stabilizers.
The interaction mechanism of zein and lysozyme was investigated via multiple analytical methods combining with molecular dynamics simulations in this study. The results showed that the zein-lysozyme complex nanoparticles with a ratio of 2:1 were stable at pH 4.0. The electrostatic and hydrophobic interactions were the main driving forces for the formation of zein-lysozyme complexes. Hydrogen bonding also existed in the nanoparticles, but not the main driving force. Images of transmission electron microscope (TEM) showed the aggregation of samples, and the field emission scanning electron microscopy (FE-SEM) images showed that the surface morphology changes from smooth to rough and irregular. Molecular dynamics simulations elucidated that lysozyme preferred to bind to the protruding area of zein. The residues of P192, A193, A194, Y195, L196, Q198, L199, N203, Q245, and L253 in zein and the residues of D49, Y63, W64, A108, W109, and V110 in lysozyme contributed the most. These results can provide a scientific guideline for the potential application of zeinlysozyme nanoparticles as delivery systems or emulsion stabilizers in food industry.
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