Interfacial properties of heat-treated ovalbumin.
The interfacial properties (kinetics of adsorption at the air/water interface, rheology of the interfacial layer) of ovalbumin molecules, unheated or previously heat-denatured in solution (10 g L(-1), pH 7, NaCl 50 mM) under controlled conditions (up to 40 min at 80 degrees C), were investigated. Heat treatments induced the formation of covalent aggregates which surface exhibits a higher hydrophobicity and an increased exposition of sulfhydryl groups when compared to native ovalbumin (unheated). Although they have a larger hydrodynamic size, aggregates adsorb as fast as native ovalbumin at the air/water interface. However, aggregates are able to established rapid contacts in the interfacial layer as shown by the fast increase of both surface pressure and shear elastic constant. In contrast, native ovalbumin needs longer time to developed intermolecular contacts and exhibits lower foam stability even if the shear elastic constant on aging reached higher value than for ovalbumin aggregates.
Croguennec
Thomas
T
INRA-Agrocampus, UMR1253, Science & Technologie du lait et de l'oeuf, 65 rue St Brieuc, F-35000 Rennes, France. thomas.croguennec@agrocampus-rennes.fr
Renault
Anne
A
Beaufils
Sylvie
S
Dubois
Jean-Jacques
JJ
Pezennec
Stéphane
S
D000327:Adsorption; D000388:Air; D000818:Animals; D004548:Elasticity; D005524:Food Technology; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D010047:Ovalbumin / Q000737:chemistry*; D010316:Particle Size; D011489:Protein Denaturation; D012212:Rheology; D012996:Solutions; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013499:Surface Properties; D013500:Surface Tension; D014867:Water
D012996:Solutions; D013438:Sulfhydryl Compounds; D014867:Water; D010047:Ovalbumin