Impact of controlled shearing on solubility and heat stability of pea protein isolate dispersed in solutions with adjusted ionic strength. (November 2019)

• Record Type: Journal Article
• Authors: Bogahawaththa, Dimuthu; Chau, Nguyen Hoang Bao; Trivedi, Jigar; Dissanayake, Muditha; Vasiljevic, Todor
• Is Part Of: Food research international. Volume 125(2019)
• Publication Date: 2019-11
• Subjects: Plant protein -- Shear -- Thermal processing -- pH -- Secondary structure -- Protein aggregation; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2019.108522
• Languages: English
• ISSNs: 0963-9969

Abstract

Abstract: 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. Graphical abstract: Unlabelled Image Highlights: High shear greatly improved solubility of pea protein isolate (PPI) during heating. Solubility was greater at unaltered ionic strength regardless of other factors. Heating cum shearing at 100 s −1 mostly resulted in insoluble covalent aggregates. Heating cum shearing at 1500 s −1 mainly formed soluble hydrophobic aggregates. Shear impacted on heat stability of PPI in a similar pattern as to the solubility.