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Impact of controlled shearing on solubility and heat stability of pea protein isolate dispersed in solutions with adjusted ionic strength
- Bogahawaththa, Dimuthu, Chau, Nguyen Hoang Bao, Trivedi, Jigar, Dissanayake, Muditha, Vasiljevic, Todor
- Food research international 2019 v.125 pp. 108522
- dispersions, food industry, food processing, heat, heat stability, hydrophobicity, ionic strength, pH, pea protein, protein isolates, solubility
- Pea protein isolates (PPI) have sustained an increasing demand in the food industry as a substitute for animal-origin proteins. Shearing is an integral part of food processing that can change properties of proteins and their functionality. PPI dispersions prepared at 4 or 8% concentration (w/w protein), pH 6.8 or 7.5 and under ionic strength (IS) 100, 200 mM or non-adjusted, were subjected to controlled shearing at two levels (100 or 1500 s−1) during heating at 90 °C for 5 min. All main factors had substantial effects on the tested dependent variables. Shearing at 1500 s−1 significantly improved the solubility and heat stability of 4% PPI at pH 6.8 or 7.5 and IS-100 or 200 mM by 27–43% in comparison to 100 s−1. Following 1500 s−1 treatment, all PPI dispersions showed >85% solubility and heat stability except 4% PPI at pH 6.8 and IS 100 mM (60%). Shearing appeared to alter structural and physicochemical properties of pea proteins as well nature of protein aggregation. Heating accompanied with 100 s−1 shearing mostly resulted in insoluble covalent aggregates while shearing at 1500 s−1 mainly contributed to formation of soluble hydrophobic aggregates.