Dry-heating makes hen egg white lysozyme an efficient foaming agent and enables its bulk aggregation.
Dry-heating is considered to be one of the most promising approaches to improving the functionality of food proteins. It has been shown that even if only minor structural modifications occur during dry-heating, the foaming properties of proteins are highly improved. With the recent results obtained in the field of foam stabilization by nanoparticles or protein aggregates in mind, a study was undertaken on the impact of dry-heating of lysozyme, used as a model protein, on its foaming properties. This work highlighted the fact that dry-heated hen egg white lysozyme simultaneously exhibited enhanced foaming properties and aggregation capacity. Although the conditions that favored bulk aggregation (high ionic strength, pH, treatment duration, and protein concentration) also favored foaming properties, the large bulk aggregates were not essential to obtain the best functionality. It is envisaged that heat-treated lysozyme may self-associate at the air/water interface, stabilizing air bubbles.
UMR1253, Science et Technologie du Lait et de l'Oeuf, INRA, Agrocampus Rennes, 35000 Rennes, France. yann.desfougeres@agrocampus-rennes.fr
Yann
Y
Desfougères
Valérie
V
Lechevalier
Stéphane
S
Pezennec
Franck
F
Artzner
Françoise
F
Nau
D000818:Animals; D002645:Chickens; D005260:Female; D005511:Food Handling; D019649:Food Industry; D006361:Heating; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*; D012995:Solubility; D013499:Surface Properties; D013997:Time Factors
C421864:hen egg lysozyme; D009113:Muramidase