Fractionation and electrophoresis of tomato waste seed proteins

Proteins of deoiled meal and alkali-extracted concentrate of tomato seeds were classified by successive extractions with sodium chloride (0.5 M), aqueous ethanol (70%) and acetic acid (0.05 M) into albumin, globulin, gliadin and glutenin. The globulin was the major protein in both meal and alkali-extracted concentrate. Native and sodium dodecylsulphate polyacrylamide gel electrophoresis of various fractions of seed meal and alkali extracted concentrate revealed that the proteins were made up of sub-units of lower molecular weights. It also indicated that different solvents extracted proteins having different molecular weights.