Abstract
Combined effects of pH-shifting and an autoclaving cycle (121 °C, 15 min) on red kidney bean lectin (RKBL) were investigated using intrinsic and extrinsic fluorescence, UV, FTIR, DSC, SEC, dot-blot analysis and in vitro digestibility. Spectroscopic studies suggested that the protein refolding was stable after 3 h incubation with the hydrophobic exposure after pH-shifting, and hydrophobicity was significantly increased with the formation of more looser structure, which would influence the structural stability of known epitopes. In details, the increase of β-turn and reduction of random coil was related with the lower denaturation enthalpy, while the protein aggregation was also observed in acidic treated samples after autoclaving. Lower antigenicity and good digestibility suggested the exposure of enzyme cutting sites, and confirmed the effectivity of pH-shifting prior to the autoclaving. Then the results would be beneficial to the development of hypoallergenic kidney bean foods.
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