Electrostatic complexation of β-lactoglobulin aggregates with κ-carrageenan and the resulting emulsifying and foaming properties

Abstract

The electrostatic complexation of protein and polysaccharide and the functional properties of the complexes are significantly affected by the structure of protein aggregates and are important in the development of new food ingredients. In this work, natural globular β-lactoglobulin (NGBLG), β-lactoglobulin nanoparticles (BLGNP), and β-lactoglobulin fibrils (BLGF) were prepared and complexed with κ-carrageenan (κ-car). Phase diagrams of the NGBLG-, BLGNP-, and BLGF-κ-car systems were established and divided into 4 regions: mixed soluble polymers (I), intramolecular soluble complex (II), intermolecular soluble complex (III), and intermolecular insoluble complex (IV). Aggregation shifted the boundaries of regions III and IV of BLGF-or BLGNP-κ-car to lower pH and higher protein aggregates/κ-car weight ratio (r), especially for BLGF-κ-car. The emulsifying and foaming properties of the 3 mixed systems were investigated in regions I and II. Complexes in region II had significantly better emulsifying properties than the corresponding mixtures in region I and the pure protein aggregates. Interestingly, phase separation resulted in different effects on the foaming properties of the 3 BLG-κ-car complexes, in which BLGF-κ-car complexation in region II decreased the foaming properties in region I but the complexation of NGBLG-κ-car and BLGNP-κ-car in region II increased the foaming properties. The BLGF-κ-car complex in regions I and II provided the best emulsifying and foaming properties. Interfacial data both on oil-water and air-water interfaces overall explained the emulsifying and foaming properties of the complexes.

Effect of Xanthan Gum, Kappa–Carrageenan, and Guar Gum on the Functional Characteristics of Egg White Liquid and Intermolecular Interaction Mechanism

“…The aggregation of protein–polysaccharide complexes significantly affects the functional characteristics of the protein so that it can be an effective emulsifier or foaming agent [ 51 ]. In Figure 9 a, the green fluorescent area indicates egg white protein, and the black area indicates polysaccharides or water.…”

A review on solubility enhancement technique for pharmaceutical drugs

“…The shape of protein aggregates has a vital function in the electrostatic complexation of protein and polysaccharide, as well as in determining the functional qualities of the resulting complexes. These interactions are of great significance in the advancement of novel dietary components [50]. In order for medications to be effective when taken orally or applied topically to the eye, they need to have a certain level of solubility in water.…”

Amyloid fibril-based membranes for PFAS removal from water

“…Moreover, the membrane surface charge is set by the amyloid fibrils since the protein fully covers the CA support membrane. The isoelectric point of BLG amyloid fibrils is around 5, which means that the pure amyloid-fibrils are negatively charged at pH 7 and positively charged at pH 2 [26][27][28] . These indications suggest that PFASs may undergo electrostatic adsorption onto proteins whose surface charge is positive at pHs below the isoelectric point (~ pH 5) 26,27 .…”

“…The isoelectric point of BLG amyloid fibrils is around 5, which means that the pure amyloid-fibrils are negatively charged at pH 7 and positively charged at pH 2 [26][27][28] . These indications suggest that PFASs may undergo electrostatic adsorption onto proteins whose surface charge is positive at pHs below the isoelectric point (~ pH 5) 26,27 . Additionally, to further increase the electrostatic interaction between amyloid fibrils and PFASs, it is possible to activate the amyloid fibril membrane by rinsing with acidic water to provide the membrane with higher charge density.…”