To improve utilization of proteins as industrial materials, a realistic view of protein structures is needed to understand their performance properties. Proteins definitely do not behave as elongated organic polymers with inter-chain interactions along their length as they are single chain balls with high intra-chain bonding. Formation of an extended chain is very energetically unfavored due the loss of internal hydrophobic and polar interactions of the individual protein, and the loss of water-water bonds if the protein is to worm its chain into the water. Additionally, they are not standard colloidal adhesives due to lack of a surfactant coated surface. The protein surface contains both hydrophilic domains to act as surfactant and hydrophobic domains that encourage protein-protein interactions. Ignoring these basic factors have led to the soy adhesive literature being filled with misconceptions that have resulted in incorrect models for adhesive performance. Individual soy protein chains have their own primary, secondary and tertiary structures. Denaturation affects the secondary and tertiary structures, which alters the globular surface, but does not eliminate the proteins from forming higher complexes. The type of denaturation has a big effect on its rheological and adhesive properties.

Protein structure-property relationships

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ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.