2023
DOI: 10.1016/j.foodhyd.2023.108514
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Ovalbumin, an outstanding food hydrocolloid: Applications, technofunctional attributes, and nutritional facts, A systematic review

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Cited by 27 publications
(9 citation statements)
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“…Partially unfolded proteins can also transform into gels by forming crosslinked networks of uncoiled polypeptide fragments. The gel-forming capability of a protein is determined by its minimum gelling concentration, or the low protein concentration required to develop a gel structure [93]. Research has shown that the lowest gelling formation concentration of chickpea protein ranges from 16 to 20%, higher than that of chickpea flour, which ranges from 8 to 12% [94].…”
Section: Gelling Propertiesmentioning
confidence: 99%
“…Partially unfolded proteins can also transform into gels by forming crosslinked networks of uncoiled polypeptide fragments. The gel-forming capability of a protein is determined by its minimum gelling concentration, or the low protein concentration required to develop a gel structure [93]. Research has shown that the lowest gelling formation concentration of chickpea protein ranges from 16 to 20%, higher than that of chickpea flour, which ranges from 8 to 12% [94].…”
Section: Gelling Propertiesmentioning
confidence: 99%
“…Egg white can get adsorbed at the air–liquid interface due to its relatively high surface hydrophobicity, hence it is the dominating protein responsible for foaming. 56 Food products prepared to utilize the foamability of eggs are mostly attributed to the ability of albumin protein to encapsulate and hold air within food products. 27 The susceptible nature of OVA to surface denaturation and interfacial coagulation are factors responsible for the foaming properties of EWP.…”
Section: Factors Affecting Foaming Behavior Of Eggsmentioning
confidence: 99%
“…Of all the egg proteins, ovalbumin (OVA) is the most promising encapsulant due to its excellent properties such as gelling, digestibility, self-assembly, and amphiphilic nature. 6 It contains both hydrophilic and hydrophobic groups with excellent foaming, emulsifying, and gelation functions. 7 It exhibited excellent emulsion stability for high internal phase emulsions with strong structural integrity and intramolecular interactions.…”
Section: Introductionmentioning
confidence: 99%
“…Egg proteins, as one of the most abundant animal protein sources, have received considerable attention for developing delivery systems. Of all the egg proteins, ovalbumin (OVA) is the most promising encapsulant due to its excellent properties such as gelling, digestibility, self‐assembly, and amphiphilic nature 6 . It contains both hydrophilic and hydrophobic groups with excellent foaming, emulsifying, and gelation functions 7 .…”
Section: Introductionmentioning
confidence: 99%