2002
DOI: 10.1006/jcis.2001.8163
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Effect of Denaturation by Preheating on the Foam Fractionation Behavior of Ovalbumin

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Cited by 26 publications
(20 citation statements)
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“…For instance, it was shown that heating proteins in a dry state can improve their foaming properties [8][9][10][11]. Similar results were obtained when heating proteins in solution above their denaturation temperature [12][13][14][15][16]. Mass transport properties, protein surface hydrophobicity, protein conformational stability, greater intermolecular interactions at the interface and some modifications in the subphase properties such as an increase of viscosity leading to reduce liquid drainage from the foam, were cited in order to explain the improved foaming properties of heat-denatured proteins.…”
Section: Introductionsupporting
confidence: 74%
“…For instance, it was shown that heating proteins in a dry state can improve their foaming properties [8][9][10][11]. Similar results were obtained when heating proteins in solution above their denaturation temperature [12][13][14][15][16]. Mass transport properties, protein surface hydrophobicity, protein conformational stability, greater intermolecular interactions at the interface and some modifications in the subphase properties such as an increase of viscosity leading to reduce liquid drainage from the foam, were cited in order to explain the improved foaming properties of heat-denatured proteins.…”
Section: Introductionsupporting
confidence: 74%
“…Salts may increase the screening of charged proteins that were concentrated at the interface due to the reduction of interfacial repulsion enabling the formation of a strong viscoelastic network [9]. In addition, chemical, physical, or enzymatic modifications are interesting ways to improve protein foaming properties [10][11][12][13][14][15][16][17][18]. These modifications could alter the kinetics of protein adsorption at the interface, the time needed for the protein to rearrange upon adsorption at the interface and its ability to share intermolecular bonding with surrounding proteins.…”
Section: Introductionmentioning
confidence: 98%
“…Egg albumin is the major globular protein of chicken egg white and denatures with increasing temperature, aggregates via intermolecular interactions and then fouls on the contacted surface. It is well established that due to its polar/nonpolar nature, egg albumin can adsorb from aqueous solutions to an air-water interface and act as a surfactant by reducing the surface tension and forming cohesive films (Du, Prokop, & Tanner, 2002). This paper describes the application of the micromanipulation technique to measure the adhesive/cohesive force between egg albumin deposits and the stainless steel substrate and combines with studies of cleaning at macroscale.…”
Section: Introductionmentioning
confidence: 98%