Physicochemical studies on wheat protein foams. II. Relationship between bubble size and stability of foams prepared with gluten and gluten components

Skim acidic milk whey cryoconcentration and assessment of its functional properties: Impact of processing conditions

“…This increases viscosity and improves other rheological properties (Damodaran, 1990). The high viscosity of the film retards drainage of lamella fluid (Mita et al, 1978).…”

Interfacial Behavior of Wheat Puroindolines: Study of Adsorption at the Air–Water Interface from Surface Tension Measurement Using Wilhelmy Plate Method

“…The interfacial films are formed only by extended amphiphilic polymer segments of adsorbed unfolded proteins, rather than by compact native structure (16). The foamability of globular proteins is directly correlated with their capability to accumulate at the air-water interface as positive excess (17)(18)(19) and is a qualitative measure of how easily protein molecules are unfolded by shear stress and exposure to the air-water interface.…”

Altering functional attributes of proteins through cross linking by transglutaminase – A case study with whey and seed proteins

“…Foam formation is generally faster for more flexible random coiled structured proteins than for the tightly held structures (Halling, 1981;Damodaran, 1990). In addition increased hydrodynamic size (Damodaran, 1994), molecular weight (Mita, Ishida, & Matsumoto, 1978) and elimination of charged amino groups of lysine residues by crosslinking could improve foaming capacity. This was true in case of 11S protein fraction of sesame and b-Lg.…”