This work aims to determine changes at molecular level of plasma proteins provoked by adding cysteine (Cys, 0.025% to 0.35% w/v) as a reducing agent and their relationship with the heat-induced gel properties obtained when subsequently the solutions were submitted to a thermal treatment. Results show that adding Cys to plasma solutions at concentrations ≥0.15% actually entails modifications in the secondary structure of their main proteins, that is, serum albumin-α-helix rich-and globulin fraction-β-sheet rich. Basically, a reduction of the intensity of the infrared (IR) bands assigned to both structures takes place concomitant to an increase of extended structures that seem to act as intermediates for the subsequent protein aggregation process through nonnative intermolecular β-sheets. Cleavage of disulfide bonds is also evidenced at Cys concentrations ≥0.15% by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with the effects being directly proportional to Cys concentration. However, beneficial effects on gel hardness are gradually obtained at Cys concentrations ≤0.15%, that is, when the effects at molecular level are at most just budding, while not more improvements on this textural parameter are obtained at higher Cys concentrations. By contrast, water retention capacity is gradually diminishing as Cys concentration increases, but with a significant reduction only obtained at the highest tested concentration. These results suggest a negative effect of Cys on gel microstructure at high concentrations, which probably can be attributed to protein aggregation taking place at room temperature.
Keywords: heat denaturation; protein functionality; structure.
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