Interaction between casein and rice glutelin: Binding mechanisms and molecular assembly behaviours. (October 2020)

• Record Type: Journal Article
• Authors: He, Chengxin; Hu, Yu; Liu, Ziwei; Woo, Meng Wai; Xiong, Hua; Zhao, Qiang
• Is Part Of: Food hydrocolloids. Volume 107(2020)
• Publication Date: 2020-10
• Subjects: Protein-protein interactions -- Casein -- Rice glutelin -- Binding mechanisms -- Molecular assembly; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2020.105967
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: The present study investigated the interaction between acid casein and rice glutelin (RG) under neutral conditions. Large particle populations contain casein-RG complex which consisted of β-casein, αs1 -casein, and RG was formed. The results of multispectral studies indicated that the peptide chain and secondary structure of casein did not change during the binding process. Besides, the binding behaviours seemed to be closely related to the surface hydrophobic region of RG. Thermodynamic parameter calculations showed that the main driving forces behind this structure formation were the hydrogen bonds and van der Waals forces. On the other hand, the addition of RG caused the generation of small particle populations (~20 nm) which mainly composed of κ-casein and αs2 -casein, and such small particle populations maintained aggregation through residual calcium. Moreover, it is noting that these two particle populations can coexist stably, this finding will provide an avenue to produce, by design, casein nanoparticles. Graphical abstract: Image 1 Highlights: 1:3.2% (w/w) rice glutelin addition to providing a saturated casein binding. Casein-rice glutelin complex consists of rice glutelin, αS1, and β-casein. Addition of rice glutelin drives dissociation of casein. Structural changes of casein resulted from the release of αS2 and κ-casein.