| Abstract: | Radionuclide-labelled glycerol triolein has been used to follow the fate of triglyceride lipids during the mixing of wheat flour doughs. After removal of residual free lipid by petrol extraction, initial fractionation of freeze-dried dough identified the acetic acid-soluble protein as being the only component involved significantly in work-induced lipid binding during dough development under nitrogen, and also in lipid release on admission of air. Very little labelled lipid was found in either the water-soluble proteins or the starch residue. Sub-fractionation of the acetic acid-soluble protein by ammonium sulphate precipitation from acetic acid-urea-cetyltrimethyl-ammonium bromide (AUC) solvent showed bound lipid to be distributed almost entirely between high-molecular-weight glutenin and protein which remained soluble in the AUC supernatant even in the presence of 20% ammonium sulphate. Precipitated gliadins contained very little labelled lipid. However, significant levels were found in classical ethanol-extracted gliadin, and were traced predominantly to the same supernatant-protein owing to its solubility in aqueous ethanol. Examination of this AUC-supernatant fraction showed it to contain a hitherto unreported protein which had a molecular weight of about 9000, was strongly complexed with tri-glyceride lipid on a 1:1 molar basis and showed a tendency to aggregate in solution. Its amino acid frequency was found to differ significantly from both glutenin and purothionin, the latter containing in particular very much more cysteine than the supernatant-protein. Representing 10% or more of the total gluten, this small, highly interactive protein is responsible for a significant, if not the major, part of lipid binding activity in dough and may well have a fundamental role in the formation of an insoluble glutenin structure through both —SH and hydrophobic interaction. Accordingly, the name ‘Ligolin’ is proposed, from the Latin ligare: to bind, to tie. |
