Stability of vicilin, a legume seed storage protein, with step‐wise electrostatic modification

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Abstract
Step‐wise chemical modification of lysine residues with maleic anhydride was used to examine the influence of electrostatic perturbation on the structural integrity of vicilin from fababeans. There were no significant changes in denaturation temperature (Td), enthalpy of denaturation (ΔH) and one‐half band width (1/2 bw) values up to 63.0% modification. Exposure of hydrophobic surface residues decreased initially to 43.9% maleylation, indicative of minor conformational fluctuations with increased surface negativity. Maleylation of vicilin to 93.8% resulted in a significant decrease in ΔH and Td values and an increase in 1/2 bw and surface hydrophobicity (So) parameters. Although progressive labelling appeared to promote unfolding and subunit dissociation, maximum modification did not result in complete vicilin denaturation. The possible existence of a critical maleylation point was attributed to the cumulative effects of electrostatic repulsion and/or modification of specific key residues.

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