Functional Properties Of Egg White Proteins Research Articles

An overview of the functional properties of egg white proteins and their application in the food industry

Egg white proteins (EWPs), in addition to their nutritional values, possess excellent functional properties that facilitate their use in the food industry. This review collates the published information concerning the major functional properties of EWPs such as gelling, foaming, and emulsifying. Gelation of EWPs has several applications in various food products such as puddings and desserts. Foaming is an important element in the manufacture of the foods such as cakes, bread, meringues, and cookies. However, the application of EWPs as an emulsifier in food products is limited, and thus, various techniques and methods for improving the emulsifying ability of these proteins have been investigated. The effect of various parameters on the functional properties of EWPs and possible correlations between structure and function, with a focus on practical performance in food systems, are discussed in this paper. These findings can lead to enriching the research systems on the functional properties of EWPs and providing information for the development of new EWPs -derived/enriched food products. • Environmental conditions change hydrophilic/hydrophobic ratio of egg white proteins. • Heat treatments potentially denature egg white proteins (EWPs) and change their structure. • Emulsifying stability of egg white proteins under neutral and alkaline conditions is poor. • Electrostatic and hydrophobic interactions are important during gel formation of EWPs. • EWPs have considerable applications in foods such as meringues and cake batters.

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

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.

Effects of sonication and high-pressure carbon dioxide processing on enzymatic hydrolysis of egg white proteins

The objectives of this study were to examine the effect of sonication and high-pressure carbon dioxide processing on proteolytic hydrolysis of egg white proteins and antioxidant activity of the obtained hydrolysates. It appeared that the ultrasound pretreatment resulted in an increase in the degree of hydrolysis of the enzymatic reaction while the high-pressure carbon dioxide processing showed an inhibition effect on the enzymatic hydrolysis of egg white proteins to some extent. The antioxidant activity of the obtained hydrolysates was improved by ultrasound pretreatment of egg white proteins at the pH 8.3. Thus, the combination of ultrasound pretreatment at the pH 8.3 and subsequent enzymatic hydrolysis with alcalase at 50?C and pH 8.0 could offer a new approach to the improvement of the functional properties of egg white proteins and their biological activity.

Modification of functional properties of egg-white proteins.

Egg-white proteins are extensively utilised as food ingredients due to their unique functional properties. Several attempts have been made in order to improve the functional properties of egg-white proteins and to identify the optimal formulations for unique food products. Experimental data proves that controlled denaturation of egg-white proteins can have a beneficial impact on various functional applications in the food industry such as emulsifying ability, heat stability, and gelation. This review describes the effect of heat-induced denaturation on protein structure and functionality. Studies on the impact of Maillard reaction, which aim to elucidate the structure-function relationship of egg-white proteins, are presented. A novel approach which could be the basis for the development of new methods aiming to improve the functional properties of egg-white proteins is also discussed.