A model for vicilin solubility at mild acidic pH, based on homology modelling and electrostatics calculations.

Abstract

The crystallographic structures of jack bean canavalin and French bean phaseolin have been used to construct a homology model of the storage vicilin of cocoa. Reported molecular weights for cocoa storage protein subunits correlate with proteolysis at the site of a large hydrophilic insert in the mature protein. Burial of the hydrophobic amino acids on trimer formation is a strongly conserved feature in the vicilin family. Histidine residues also sit at the monomer-monomer interfaces of the trimer and are likely to contribute to the decreased solubility of cocoa vicilin at mild acidic pH, which is generally considered to be caused solely by aggregation near to the isoelectric point. Electrostatic calculations suggest that such an arrangement of histidine residues in the absence of specific counterion binding will not favour the particular geometry of trimer formation below neutral pH. Higher order aggregates that do not exclude histidine charge from the solvent may be favoured, aiding the precipitation of cocoa vicilin at mild acidic pH. This suggestion is considered for the vicilin family. The hypothesis could contribute to an understanding of the pH and ionic strength dependence of vicilin solubility in vitro, and possibly of the behaviour of vicilins in the seed storage environment.