Abstract

Gel network formation of a salt-extracted pea protein isolate was studied using dynamic rheological measurements. The gelling point was dependent on heating rate and was unaffected by cooling rate. When both the heating and cooling rates were increased (from 0.5 to 4 °C/min) final G′ value decreased, indicative of decreased gel strength. During the heating phase, the storage modulus and loss modulus fluctuated below 1 Pa at almost constant values with the storage modulus smaller than the loss modulus until the gelling point was reached. The rate of cooling has a greater impact on the development of storage modulus than that of heating. Compared to the gel strength of commercial pea protein isolate (PPIc) and soy protein isolate (SPIc) at the same protein concentration, salt-extracted pea protein isolate (PPIs) was much stronger than PPIc but weaker than SPIc. Careful control of the heating and cooling rates enable maximum gel strength for heat-induced pea protein gel, thus enhancing utilisation of pea protein as an additive in meat food industry.

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