Cereal Chem 55:295 - 307.  |  VIEW ARTICLE
Vegetable Protein: Lipid Interactions.

V. B. Kamat, G. E. Graham, and M. A. F. Davis. Copyright 1978 by the American Association of Cereal Chemists, Inc. 

Soybean protein, phospholipids, and neutral lipids interacted under cavitational force fields in essential accordance with the published methodology for reassembly of lipids and apoproteins of naturally occurring lipoproteins. Native soybean globulins do not form lipoproteins. Prior dissociation with denaturing agents, e.g., urea, guanidine hydrochloride, acid pH, or alkaline pH, yielding predominantly a population of subunits providing increased surface area and greater proportion of hydrophobic residues is necessary to activate the globulins to form lipoproteins of characteristic buoyant densities. This principle seems to hold true for other vegetable proteins. Denatured globulins are shown to provide greater emulsion stability than do native globulins. The pH dependence of emulsion stability has been established and results are discussed in terms of current knowledge of multisubunit vegetable proteins.