Table 5.

Effects of pulsed electric field (PEF) on the techno-functional properties of dairy proteins.

Dairy Protein	PEF Conditions	Changes in Protein Functionality	References
Raw milk	Intensity of 30 kV/cm, outlet temperature of 50 ± 1 °C; pulse number of 80 and 120 pulses, pulse width of 2 µs, and pulse frequency of 2 Hz.	Rennet coagulation time (RCT) higher than that of raw milk but lower than that of pasteurized milk.	[105]
Whey protein isolate (WPI)	15–22 V/cm heating phase and 4 to 8 V/cm holding phase, frequency of 25 kHz.	Moderate electric field treatment resulted in a weaker gel structure than conventional heat treatment.	[106]
β-lactoglobulin	20 V/cm during holding, 80 V/cm during heating, and frequency of 20 kHz.	At pH 7, moderate electric field and thermal treatment (up to 60 °C) had similar effects on the free SH group relativity. At higher temperatures, conventional heat-treated samples had higher free-SH-group relativity than moderate electric field-treated samples.	[99]
WPI	30–35 kV/cm, 19.2–211 µs, 30–75 °C.	Emulsions stabilized by PEF-treated and heat-treated (72 °C for 15 s) WPI showed similar droplet sizes and similar emulsifying properties. Increasing the duration of heat treatment to 10 min caused a significant increase in the droplet size of emulsions stabilized by heat-treated WPI. PEF-treated WPI showed lower gel strength than untreated samples. Increasing the duration of PEF further decreased the gel strength.	[95]
β-lactoglobulin	Intensity of 12.5 kV/cm with 40 µF of capacitance.	PEF improved the gelling rate of β-lactoglobulin (at 72 °C) when the number of pulses was less than six.	[31]
WPI	15 to 55 kV/cm, 2 to 8 and 50 to 90 °C.	The gelling properties of WPI increased when treated at 35 kV/cm but decreased after treatment at 45 kV/cm.	[107]