Interaction mechanism between zein and β-lactoglobulin: Insights from multi-spectroscopy and molecular dynamics simulation methods. (February 2023)

• Record Type: Journal Article
• Authors: Liu, Chengzhi; Lv, Nan; Song, Yuling; Dong, Lijuan; Huang, Min; Shen, Qing; Ren, Gerui; Wu, Ruibo; Wang, Binju; Cao, Zexing; Xie, Hujun
• Is Part Of: Food hydrocolloids. Volume 135(2023)
• Publication Date: 2023-02
• Subjects: Zein -- β-Lactoglobulin -- Interaction mechanism -- Molecular dynamics simulation -- Gibbs free energy; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2022.108226
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: The interaction of zein and β-lactoglobulin (β-LG) was explored by experiments combined with molecular dynamics simulation method. The results showed that the particle sizes of β-LG-Zein complex nanoparticles enhanced from 69.5 nm to 153.5 nm when the β-LG/zein mass ratio changed from 9:1 to 2:8. The complex nanoparticles exhibited better stability after 30 d of storage. Transmission electron microscope (TEM) showed that the β-LG-Zein nanoparticles dispersed evenly with high β-LG concentration. Fourier transform infrared spectroscopy (FTIR) and dissociation test experiments elucidated that hydrogen bonding, hydrophobic and electrostatic interactions were important for preparing β-LG-Zein complex nanoparticles. The conformational model of zein was constructed through homology modeling, and the structure of β-LG-Zein complex was obtained via molecular docking. Molecular dynamics simulation (MD) results clarified that β-LG firmly grasped zein like a clamp, taking the P68 and G88 residues of zein as the supporting point, and the binding Gibbs free energy reached −39.81 kcal/mol. In addition, the residues of V64, P65, P68, I69, G74, G75, G77 and G88 in zein and the residues of P54, L103 and A104 in β-LG played critical roles for the binding of zein to β-LG. This work can provide a theoretical foundation for the applications of β-LG-Zein complexes in food industry. Graphical abstract: Image 1 Highlights: The β-LG-Zein complex nanoparticles were fabricated by pH-shifting method. The electrostatic, hydrogen bonding and hydrophobic interactions were the main driving forces. The β-LG-Zein complex nanoparticles exhibited excellent storage stability. Key residues with big energy contribution were recognized through MD simulations.