Modification methods and applications of egg protein gel properties: A review

Abstract

Egg protein (EP) has a variety of functional properties, such as gelling, foaming, and emulsifying. The gel characteristics provide a foundation for applications in the food industry and research on EP. The proteins denature and aggregate to form a dense three‐dimensional gel network structure, with a process influenced by protein concentration, pH, ion type, and strength. In addition, the gelation properties of EP can be altered to varying degrees by applying different treatment conditions to EP. Currently, modification methods for proteins include physical modification (heat‐induced denaturation, freeze–thaw modification, high‐pressure modification, and ultrasonic modification), chemical modification (glycosylation modification, phosphorylation modification, acylation modification, ethanol modification, polyphenol modification), and biological modification (enzyme modification). Pidan, salted eggs, egg tofu, and other egg products have unique sensory properties, due to the gel properties of EP. In accessions, EP has also been used as a new ingredient in food packaging and biopharmaceuticals due to its gel properties. This review will further promote EP gel research and provide guidance for its full application in many fields.

Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin

“…Protein cross linking facilitated via disulfide bond formation is the main factor that drives the gelling of egg white. After denaturation, the sulfhydryl groups of ovalbumin and ovotransferrin become exposed to the environment, enhancing sulfhydryl reactions to form disulfide bonds, thus promoting the formation of protein gels [ 6 ]. Additionally, the high viscosity of ovomucin contributes to the gelling properties of egg white and plays an important role in gel formation.…”

“…Additionally, the high viscosity of ovomucin contributes to the gelling properties of egg white and plays an important role in gel formation. Other proteins that influence gelling of egg white include ovomucoid and lysozyme [ 6 ]. The process of formation for most gels follows the general steps of conformational change or moderate denaturation of the protein molecule followed by self-association and subsequent gelation.…”

“…Environmental conditions are generally altered to trigger this effect. The most common, especially in the case of egg white, is heat-induced gelling; others include changes in pH or salt concentration, or the addition of monovalent and/or divalent cations [ 6 , 7 ]. Formation of a stable gel is driven by covalent and non-covalent interactions, and results in a change of the surface properties, number of free sulfhydryl groups, and solubility of the denatured protein molecules [ 6 ].…”

Preparation and Properties of Egg White Dual Cross-Linked Hydrogel with Potential Application for Bone Tissue Engineering

“…Proteins undergo denaturation in response to certain external stimuli (e.g., physical factors such as heating, ultraviolet light and pressure or pH, metal ions), and denaturation is one of the important mechanisms in the formation of protein hydrogels. The gelation of egg white protein involves multiple processes, including denaturation, aggregation and formation of gel network, and the gelling properties mainly depend on the medium conditions such as pH, ionic strength and salt type [ 27 ]. The interaction and the molecular conformation of protein chains will change during protein hydrogel formation.…”

Microwave-Assisted Extraction and Ultrasound-Assisted Glycation of Ovomucoid: Structural and Functional Properties

“…The methods to reduce protein sensitization include ultrasound, heating, pulsing, phosphorylation, and acylation. ,− However, physical methods cannot significantly reduce the allergenicity of OVM because OVM is a more stable glycoprotein in structure . Therefore, a safer and more effective modification method with mild reaction conditions is needed.…”