Thermal Stability of Individual Molecular Species of Soybean β-Conglycinin

Abstract

The thermal stability of three individual molecular species of soy-bean β-conglycinin, α₃, β₃, and modified α₃ (amino terminal Val1-Arg126 amino acid groups deleted), was studied by the change in far- and near-ultraviolet CD spectra and in surface hydrophobicity. The α₃ molecule was less thermostable than β₃, its lower stability being derived from the core of the molecule rather than the extra polypeptide chain on the amino terminal side.