Determination of Molecular Weight of Soluble Ovalbumin Aggregates during Heat Denaturation Using Low Angle Laser Light Scattering Technique

Influence of Sodium Chloride and Glucose on the Aggregation Behavior of Heat‐Denatured Ovalbumin Investigated with a Multiangle Laser Light Scattering Technique

“…Therefore, further experiments were performed using 0 to 10 mM NaCl. Kato and others (1983) reported that ovalbumin dissolved in 1/15 M phosphate buffer, pH 7.4, containing 100 mM NaCl did not coagulate under heating at 80 °C, whereas ovalbumin heated in the presence of more than 10 mM NaCl did coagulate in our experiment. One possible cause of this discrepancy is the different protein concentration and heating time.…”

“…One possible cause of this discrepancy is the different protein concentration and heating time. Kato and others (1983) heated 0.05% to 0.25% ovalbumin solutions for approximately 30 min, whereas we heated 2% ovalbumin solution for 1 h.…”

Viscoelastic Properties of Whey Protein Gels: Mechanical Model and Effects of Protein Concentration on Creep

“…This general definition has caused some confusion in the food science field. Gels made from gelatin and agar-agar have been considered "true" gels, whereas heat coagulated egg white is not considered a "true" gel (Kuwahata and Nakahama, 1975;Foegeding et al, 1986), but a coagulum (Shimada andMatsushita 1980, 1981;Kato et al, 1981Kato et al, , 1983Goldsmith and Toledo, 1985). Whey proteins can form both coagula and gels depending upon composition and gelling conditions (Mulvihill and Kinsella, 1988a).…”

Application Potential of Food Protein Modification

“…Aggregates and gel networks are often the result of combined action of hydrophobic and electrostatic interactions and covalent interactions, in the form of disulfide bonds, are sometimes present (Kato et al, 1983;Koseki et al, 1989;Sun & Hayakawa, 2002). Thiolation of ovalbumin mediated through the reaction of S-acetylmercaptosuccinic anhydride (S-AMSA) with primary amines results in the formation of acetylthio groups and the acetyl group can be cleaved off to yield reactive sulfhydryl groups by the addition of hydroxylamine (Klotz & Heiney, 1962).…”

“…Disulfide bonds are thought to play a crucial role determining the stability of proteins (Betz, 1993;Zavodszky et al, 2001; reviewed by Creighton, 1988) as well as to impact on the aggregation process and gel formation of various proteins including ovalbumin (Broersen et al, 2006;Kato et al, 1983), vicilin (Arntfield et al, 1991), and -lactoglobulin (Sawyer, 1968). Aggregates and gel networks are often the result of combined action of hydrophobic and electrostatic interactions and covalent interactions, in the form of disulfide bonds, are sometimes present (Kato et al, 1983;Koseki et al, 1989;Sun & Hayakawa, 2002).…”