Effect of polysaccharides on the functional properties of egg white protein: A review

Abstract

Egg white protein (EWP) was one of the high‐quality protein sources and widely used in the food industries because of excellent emulsifying, gelling, and foaming properties. Polysaccharides as a natural biological macromolecule have been used to improve the functional properties of EWP. The electrostatic interaction was the main driving force between EWP and polysaccharides. However, protein‐polysaccharides complexes were susceptible to environmental factors including pH, ionic strength, polymer ratio, and temperature. In this paper, the functional properties of EWP were summarized. More importantly, the effects of polysaccharides on the functional properties of EWP were highlighted and reviewed referring to emulsifying, foaming, and gelling properties. The impact of environmental factors on the protein‐polysaccharides interaction were also discussed. This paper leaded to enrich research systems of protein‐polysaccharides interaction and provided information for the development of new egg white‐derived foods.

A Vital Role of High-Pressure Processing in the Gel Forming on New Healthy Egg Pudding through Texture, Microstructure, and Molecular Impacts

“…Pudding treated with 450 MPa for 5 min showed the highest syneresis percentage, which may be due to high-pressure levels at 450 MPa, caused by weak gel, and the inability to form a strong three-dimensional network structure, as verified from microstructure observations. Another possible explanation for high syneresis may be low pH levels, which was 4.33 and far from the isoelectric point (4.5) of albumin [ 26 ]. Therefore, the increasing positive charge of protein led to fewer binding sites for water.…”

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

“…The polysaccharides were not inclined to be adsorbed to the air–water interface because of their high hydrophilicity; however, they were combined with egg white protein to cause the hydrophilic region of the protein to further protrude into the aqueous phase, which produced strong steric hindrance protection and inhibited disproportionation and coalescence of bubbles, thereby strengthening FS [ 17 ]. More importantly, XG and GG could promote intermolecular interactions to enhance the liquid viscosity, slowing the foam film rupture caused by drainage, which also contributed to FS [ 20 ]. Therefore, the FS of EWL + XG and EWL + GG groups was improved.…”

“…Urea and NaCl were selected as hydrogen bond-breaking and electrostatic-interfering agents to explore the effect of hydrogen bonding and electrostatic interactions on the apparent viscosity of the liquid, which could characterize the intramolecular or intermolecular interactions between polysaccharides and proteins [36,37]. With the addition of NaCl to the mixture, Clcompeted with the negative polysaccharides for the binding sites of positively charged proteins, and Na + competed with the positively charged proteins for the binding sites of the negative polysaccharides, which shielded the electrostatic attraction between the negative polysaccharides and proteins [20]. Because of their ability to form strong hydrogen bonds, urea functional groups preferentially adsorb onto protein hydrophilic residues through hydrogen bonds, reducing the intramolecular and intermo- Urea and NaCl were selected as hydrogen bond-breaking and electrostatic-interfering agents to explore the effect of hydrogen bonding and electrostatic interactions on the apparent viscosity of the liquid, which could characterize the intramolecular or intermolecular interactions between polysaccharides and proteins [36,37].…”

Antibacterial Soy Protein Isolate Prepared by Quaternization

“…After the QSPI was dissolved in deionized water at pH = 2, 7, and 13 with a concentration of 10 mg/mL, the water solubility of the QSPI was measured by the UV spectrophotometer at the absorbance of 280 nm [ 33 ]. The SPI could be dissolved thoroughly when the pH ≥ 11 and the absorption of QSPI in deionized water with pH = 13 was used as control [ 34 ].…”