Characterization of soybean proteins-fatty acid systems

Abstract

This study investigated, with the aim of obtaining more flexible and hydrophobic proteins, the attachment of a low chain fatty acid, decanoic acid, to alkaline and acid soybean proteins; and the effect on their conformational and functional properties. The extent of esterification was high at acid pH and also increased with heating. Protein solubility decreased, mainly at the highest temperature (60 _C). Increasing levels of fatty acid formed a complex with a slightly more soluble protein with less surface hydrophobicity. Esterified proteins exhibited aggregation/dissociation and were stabilized by different protein subunits belonging to 7S and 11S globulins. Denaturation of these soybean protein fractions (7S and 11S) were also detected in these complexes. The highest level of fatty acids favored formation of a more ordered protein structure.