Abstract
The solubility, intrinsic viscosity ([η]), and sedimentation behavior of a lupin protein system extracted from Lupinus luteus seeds have been determined. The results were compared with those published in the literature for soy proteins. The relationship between solubility and pH for the lupin protein isolate was similar to that reported in literature for soy isolates. The [η] of the lupin protein isolate was ∼7 mL/g. These values are comparable to those obtained by other authors for soy proteins. Sedimentation velocity studies suggested that there are three main globulins in lupin protein with sedimentation coefficients of 13, 7, and 2 S. The molar mass of the major lupin globulin (390 000 g/mol) was slightly higher than reported for the soy 11S globulin (340 000 g/mol), but the lupin 7S component gave a much smaller value (105 000 g/mol) than the soy 7S (180 000 g/mol). The consequences in thickening and thermal gelation properties of the lupin protein system are discussed. Keywords: Lupin proteins; solubility; intrinsic viscosity; molar mass
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