Formation and structure of whey protein heat-induced gels (100 mg mL-1) through heat treatment at 80 °C and pH modifications at three pH values of acidic (2), isoelectric (5.6) and neutral (7) were studied. The obtained results indicated that the nature of the primary gel networks was different at each pH value. The heat-induced gels produced at pH of 2 and 7, had acceptab...

This experiment was carried out to study the flow properties of whey protein (WP) dispersions as influenced by pH and protein concentration. All WP dispersions showed shear thinning behaviour around the ambient temperature which was not affected by pH at low protein concentrations (10%). Consistency coefficient of the dispersions was significantly (P < 0.05) affected by pH while the flow behavi...

The rheological properties, structure and potential synergistic interactions of whey proteins (1-6%) and inulin (20%) in mixed gels in the presence of CaCl2 was the aim of this study. Whey proteins have a strong influence on inulin gel formation. At low concentrations (2%) whey proteins did not impair in inulin gel formation. At higher concentration (4%) whey proteins impaired inulin gelation a...

Milk was thermally processed by Ultra-High-Temperature (UHT, 132 to 154 C for 0 to 12 sec) and Vat (VAT, 66 C to 88 C for 0 to 30 min) systems. Representative milks were fermented into gels by a traditional yoghurt fermentation procedure. Selected functional properties, i.e. whey protein denaturation, gel strength, and their interrelationship were studied. Denaturation behavior of the five whey...

The effects of heat-induced denaturation and subsequent aggregation of whey protein isolate (WPI) solutions on the rate of enzymatic hydrolysis was investigated. Both heated (60 °C, 15 min; 65 °C, 5 and 15 min; 70 °C, 5 and 15 min, 75 °C, 5 and 15 min; 80 °C, 10 min) and unheated WPI solutions (100 g L(-1) protein) were incubated with a commercial proteolytic enzyme preparation, Corolase PP, un...

Abstract The effects of heat treatment (90 °C, 5 or 30 min) and enzymatic crosslinking with transglutaminase (TG, 10, 100 1000 nkat/g protein) on emulsifying gelling properties faba bean protein isolate (FPI) were studied. Heat FPI caused a clear shift in far-UV CD spectra towards random coil structure an increase surface hydrophobicity from 181 to 504 RFU. TG crosslinked heat-treated more effi...