Gelation Properties of Pea Protein Isolate underwent pH-shifting Treatment

doi:10.7506/spkx1002-6630-201321003

Abstract

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) (P ＜ 0.05). 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.

Key words: pea protein isolate, pH-shifting treatment, gelation strength, subunit composition, dynamic rheology

CLC Number:

TS229

JIANG Jiang1，LI Kai-fang1，LIU Yuan-fa1,*，XIONG You-ling L.2. Gelation Properties of Pea Protein Isolate underwent pH-shifting Treatment[J]. FOOD SCIENCE, 2013, 34(21): 10-15.

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