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- W3149485375 abstract "The tertiary structure of pea protein can be modified by pH-shifting treatments to bring about enhanced functional properties.To exploit the application potential of pea protein isolate(PPI) as a novel protein ingredient,this research focused on the gelation properties of PPI under different processing treatments.The minimum gelling concentration(MGC) was reduced from 16 g/100 mL for native PPI to 14 g/100 mL after either acid(pH 1.5) or alkaline(pH 12) treatment.These three types of PPI were subjected to 0.1 mol/L and 0.6 mol/L NaCl or 5,10 mmol/L and 20 mmol/L CaCl2,and the samples with 0,0.1 mol/L NaCl and 10 mmol/L CaCl2 were also treated with 0.1% microbial transgluaminase(TGase) to elucidate the effect of salts and TGase on gel strength.It was found that the pH 12 treatment markedly improved the PPI gel strength(up to 9 fold),and the presence of TGase further enhanced the gelling potential of PPI(by 11 fold)(P0.05).Dynamic rheology tests showed greater shear storage(G') and loss(G) moduli for pH 12 treated PPI than for untreated SSP at all oscillatory frequencies tested(0.1—10 Hz),indicating stronger intermolecular interactions in the protein matrix of the thermal gels comprised of alkaline pH-treated PPI." @default.
- W3149485375 created "2021-04-13" @default.
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- W3149485375 date "2013-01-01" @default.
- W3149485375 modified "2023-09-24" @default.
- W3149485375 title "Gelation Properties of Pea Protein Isolate underwent pH-shifting Treatment" @default.
- W3149485375 hasPublicationYear "2013" @default.
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