In this work, we investigated PEGylated black kidney bean protein isolates (BKBPI) by PEG succinimidyl carbonate (PEG-SC), PEG succinimidyl succinate (PEG-SS) and PEG succinimidyl propionate (PEG-SPA) conjugation. The functional properties, thermodynamic stability, in vitro digestion stability, and hemagglutination activity of the modified products were evaluated. The degree of PEGylation was measured, and FTIR analysis revealed that protein-PEG conjugations were formed, and that no obvious changes in water- and fat-holding capacities were observed. The solubility, emulsifying property, and foaming property were all improved through the modification, while, higher thermodynamic stability was achieved with the increase in Td values and reduction of ΔH. The PEGylated proteins were found to be more resistant to in vitro digestion, and the hemagglutination activity was significantly (P < 0.05) decreased, indicating the higher safety of the protein isolate. The results showed that the functional properties, thermodynamic stability, and biological safety of BKBPI were improved by PEGylation, which could serve to increase the applications for this protein.
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