Surface hydrophobicity changes and heat-induced modifications of .alpha.-lactalbumin

Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis

“…Griko, Freire, and Privalov (1994) reported that ALA is in a compact intermediate state or molten globule state at pH 3. At room temperature, apo-ALA (without Ca 2+ ) showed a higher number of ANS binding sites compared to the halo-form (with Ca 2+ ) (Eynard, Lametti, Relkin, & Bonomi, 1992).…”

Application of differential scanning calorimetry in food research and food quality assurance

“…Thermal stability of several proteins of interest to the food industry were investigated indeed by DSC as affected by various environmental factors. Studies on egg proteins such as ovalbumin [8,9], conalbumin [10] and lyzozyme [11], milk proteins such as beta-lactoglobulin [12][13][14], ot-lactalbumin [15,16] and casein, as well as muscle proteins such as myosin and actin [17,18] and plant proteins such as vicilin from faba beans [8] and rapeseed storage protein [19], and globulins isolated from various cereal grains [20] can be mentioned.…”

Digestibility and structural parameters of spray-dried casein clusters under simulated gastric conditions

“…A larger difference in the SH values between the specimens dried with 150°C and 180°C was observed in A70, approximately 27% increase, compared to A60 (23%). It was reported that a heat-induced rise in SH was observed in milk proteins, and it was caused by the denaturation of their tertiary and secondary structures (Euston, Ur-Rehman, & Costello, 2007;Eynard, Iametti, Relkin, & Bonomi, 1992;Risso, Borraccetti, Araujo, Hidalgo, & Gatti, 2008;Sava, Van der Plancken, Claeys, & Hendrickx, 2005). When adjusting the pH of a milk protein solution, the change in SH value was observed to be closely linked with their solubility and functional properties (Alizadeh-Pasdar & Li-Chan, 2000;Shimizu, Saito, & Yamauchi, 1985;Voutsinas, Cheung, & Nakai, 1983).…”