Abstract
Spray‐dried whey protein isolate (WPI) powders were prepared at pilot‐scale from solutions without heat (WPIUH), heated (WPIH) or heated with calcium (WPIHCa), which were analysed and compared with a control sample (WPIC). WPIC, WPIUH, WPIH and WPIHCa solutions had whey protein denaturation levels of 0.0, 3.2, 64.4 and 74.4%, respectively. Computerised tomography scanning showed that 52.6, 84.0, 74.5 and 41.9% of WPIC, WPIUH, WPIH and WPIHCa powder particles had diameters of ≤30 µm. WPIHCa and WPIH powders were cohesive, while WPIC and WPIUH powders were easy flowing. Marked differences in microstructure were observed between WPIH and WPIHCa. There were no measured differences in wall friction, bulk density or colour.
Highlights
In the food industry, demand for high-protein dairy powders, such as whey protein isolate (WPI), has been increasing over the last decade (Lagrange et al 2015)
The total denatured protein levels were 3.2, 64.4 and 74.4% for WPIUH, WPIH and WPIHCa, respectively. These values are in agreement to those reported in the work of Joyce et al (2017) who observed increasing whey protein denaturation as temperature increased in wheydominant infant formula systems
It was found that samples with final viscosity >100 mPa.s gelled within 24 h of thermal treatment, which coincides with previous findings of Joyce et al (2018) and Phan-Xuan et al (2014), who investigated viscosity and denaturation of thermally processed WPI and b-lg solutions with added calcium, respectively
Summary
Demand for high-protein dairy powders, such as whey protein isolate (WPI), has been increasing over the last decade (Lagrange et al 2015). This is because these powders provide a high-quality protein source and have a wide range of functional properties desired during processing and in finished product applications. Heat- and mineral-induced aggregation of b-lg allows for disulphide bonding and electrostatic shielding/salt bridges to form within and between whey protein molecules. Whey proteins can form different structures (e.g. strands, fibrils) depending on the exact thermal processing parameters employed (Akkermans et al 2008)
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