Study of the stability of egg white protein-based foams: effect of heating protein solution

✍ Scribed by Natahlie Hagolle; Perla Relkin; Yves Popineau; Dominique Bertrand

• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 341 KB
• Volume: 80
• Category: Article
• ISSN: 0022-5142
• DOI: 10.1002/1097-0010(200006)80:8<1245::aid-jsfa631>3.0.co;2-4

✦ Synopsis

The results reported in this study are concerned with the effects of pre-heating treatments of ovalbumin and lysozyme solutions on the formation, stability and texture morphology of their corresponding foams. It was shown that pre-heating solutions of these proteins to temperatures higher than that of their thermal denaturation led to an enhanced rate of surface pressure development and enhanced foaming properties relative to the unheated proteins. The effect of pre-heating was more clearly apparent for lysozyme, which has a higher rigidity than ovalbumin in the native conformational state. Furthermore, the evolution of liquid volume retained in the lysozyme-and ovalbumin-based foams and foam images during the destabilisation step indicated the slowest drainage and the ®nest, most homogeneous and most stable foam texture for foams formed from pre-heated protein solutions.