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To elucidate the conformational stability of proteins in colloidal food system, molecular properties of various proteins such as chemically modified β-lactoglobulin, bovine serum albumin (BSA) structural intermediates, and β-casein under chaotropic conditions, were examined using circular dichroism, SS bond content, and hydrodynamic radius determination. As refolding time increases, BSA intermediates approach the conformation of native BSA. And succinylation made β-lactoglobulin have more aperiodic structure by increasing net negative charge. Also, under chaotropic conditions, the conformation of (3-casein was affected by hydrophobic interactions. This study clearly indicates that hydrophobic interactions and electrostatic interactions are major contributing factors in conformational stability of proteins.
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