Conformational transition and gelation of κ-carrageenan in electrostatic complexation with β-lactoglobulin aggregates. (September 2021)

• Record Type: Journal Article
• Authors: Hu, Bing; Hu, Jing; Han, Lingyu; Cao, Jijuan; Nishinari, Katsuyoshi; Yang, Jixin; Fang, Yapeng; Li, Dongmei
• Is Part Of: Food hydrocolloids. Volume 118(2021)
• Publication Date: 2021-09
• Subjects: Conformational transition -- Gelation -- Electrostatic complexation -- Aggregates; Hydrocolloids -- Periodicals; Food additives -- Periodicals; Colloïdes -- Périodiques; Aliments -- Additifs -- Périodiques; Colloids; Food additives; Periodicals; Electronic journals; 664.06
• DOI: 10.1016/j.foodhyd.2021.106764
• Languages: English
• ISSNs: 0268-005X

Abstract

Abstract: The goal of this study was to evaluate the impact of electrostatic complexation with three different β-lactoglobulin aggregates on the conformational transition and gelation of κ-carrageenan (κ-car). We prepared native granular β-lactoglobulin (NGBLG), nanoparticle β-lactoglobulin (NPBLG), and fibrillary β-lactoglobulin (FBLG), and then assessed their electrostatic complexation with κ-car and the resultant impact on κ-car conformational transition, gelation, and microstructural changes. A quantitative model based on the McGhee-Hippel theory was adopted as a means of describing the impact of electrostatic complexation on the κ-car conformational transition in the presence of these protein aggregates. FBLG resulted in the most significant inhibition of κ-car conformational transition and gelation, whereas NPBLG had the least significant impact on this process. This was attributed to the fact that NPBLG imposed the least steric hindrance of these three aggregates. Together, these data highlight promising approaches to regulating polysaccharide gelation, viscoelasticity, rheological behavior, and conformational transition for use in a range of industrial applications. Graphical abstract: Image 1 Highlights: Evaluated the gelation of κ-car complexation with three β-lactoglobulin aggregates. Prepared native granular β-lactoglobulin and its aggregates NPBLG and FBLG. FBLG resulted in the most significant inhibition of κ-car gelation. A quantitative model was adopted to describe electrostatic complexation.