Protein–lipid interactions in gluten elucidated using acetic acid fractionation

Protein–lipid interactions in dough have an important impact on the quality of bakery products. Understanding of protein–lipid interactions in gluten can enhance the development of technological solutions to improve the breadmaking quality of flour as well as the functional properties of gluten. In this study, acetic acid at two different concentrations was used for treating and fractionating gluten. The impact of these procedures on the distribution of lipid components was measured. Acetic acid was able to dissociate non-polar lipids from the gluten protein matrix. Upon fractionation monomeric proteins (predominantly gliadins) and phospholipids were high in the 0.01 M acetic acid soluble fraction. The subsequent fractionation step using 0.1 M acetic acid resulted in an increased amount of high-molecular-weight glutenin subunits (HMW-GS) in the soluble fraction, along with more non-polar lipids and glycolipids in both the free and bound lipid extracts. The distribution of lipid classes demonstrates that non-polar lipids are either associated with the glutenin polymeric network through hydrophobic interactions or entrapped within the gluten matrix. The results also indicate that in gluten, glycolipids are likely to be associated with glutenins through both hydrophobic interactions and hydrogen bonds whilst phospholipids preferentially interact with gliadins and lipid binding proteins.