ABSTRACT
Peanut proteins are mostly composed of arachins and conarachins, globular proteins that can form gels under thermal denaturation or enzymatic treatment. We explored here how ionic strength (0.5 M or 0.8 M) and gelation process (a thermal treatment preceded or not by an enzymatic pre-treatment) could affect peanut protein gel properties. Gel formation and final properties were characterized by rheology, and gel structure was observed by confocal microscopy. We found that the ionic strength imposed during protein extraction determines the arachins/conarachins ratio, and that conarachins-rich samples give stronger gels, which is attributed to their higher content in free thiol groups and lysine residues. The gel storage modulus exhibited a power-law dependence with the protein concentration, which exponent depended on the gelation process. Rheological results, together with confocal microscopy imaging, showed that an enzymatic pre-treatment resulted in denser structures than when a simple thermal treatment was applied.