Gelation behavior of protein isolates extracted from 5 cultivars of Pisum sativum L

Protein isolates were extracted from 5 pea (Pisum) cultivars and their gelation behaviors were compared at pH 7.6. Gel formation and development was monitored via constant oscillation dynamic measurements. The standard heating and cooling rate was 1.0°C/min, but samples were also heated at 0.5°C (and cooled at 1.0°C/min) and others were heated...

Heat-induced gelation of pea legumin: Comparison with soybean glycinin

Gel network formation of pea legumin (8.4% on a protein basis, pH 7.6) was monitored via dynamic rheological measurements. Gelation was performed in the absence and presence of the thiol-blocking reagent N-ethylmaleimide, at different rates of heating and cooling. Overall, it was shown that pea legumin gel formation was not effected by changes...

Characterization of Pea Vicilin. 1. Denoting Convicilin as the α-Subunit of the Pisum Vicilin Family

Vicilin, a major globulin protein of pea that has been described as "extremely heterogeneous in terms of its polypeptide composition", was extracted from pea flour under alkaline conditions and subsequently fractionated by salt under acid conditions. This procedure induced the separation of vicilin into two fractions, which, after purification,...

Characterization of Pea Vicilin. 2. Consequences of Compositional Heterogeneity on Heat-Induced Gelation Behavior

The gelling characteristics of two vicilin fractions from pea (Pisum sativum L.) were compared over a range of pH and salt conditions after preliminary results showed that despite having equal opportunity to unfold, and expose hydrophobic residues, they had different minimum gelling concentrations (at pH 7.6). Furthermore, at this pH one...

Protein-induced tecture formation in novel protein foods