Combined effects of pH and thermal treatments on IgE-binding capacity and conformational structures of lectin from black kidney bean (Phaseolus vulgaris L.).

Abstract Combined effects of pH and thermal treatments on black kidney bean lectin (BKBL) were investigated by response surface methodology (RSM). Low-pH (1.0, 2.0, 3.0) incubation decreased hemagglutination activity (HA) and IgE-binding capacity, but the activities would be restored when the lectin was treated by pH shifting to 7.2. Conformational structure analyses indicated that low-pH induced protein unfolding and pH-shifting treatment resulted in a limited structural rearrangement. Mild heating, such as 60 °C for 3 min, slightly increased the HA and IgE-binding activities of pH shifted BKBL, but no obvious effects in the pH 1.0 incubated BKBL. High-temperature and long-time treatment might induce the protein aggregation, further decreased HA and IgE-binding capacities. RSM results showed both IgE-binding capacity and HA were the lowest under the combination of pH 1.0 incubation with 80 °C heating for 15 min or pH shifting from 1.0 to 7.2 with 100 °C heating for 10 min.