Electrophoretic studies for determining soy proteins xanthan gum interactions in foams

The aim of this work was to elucidate soy proteins-xanthan gum interactions at a molecular level by studying protein composition at the air-water interface of foams and in the solutions used to make them and to see if the different properties of heat denatured protein were reflected in the proportions in which they were present at the interface or in the ability to interact with xanthan. To this end SDS-PAGE and densitometry was employed. Initial protein concentration and xanthan influenced the composition of proteins in the solutions used to make the foams. The increase in NSP concentration of solutions (0.5-6 wt.%) in the absence of xanthan promoted the formation of aggregates of low molecular weight (160 kDa), the association of A an B polypeptides and a decrease in alpha and alpha' subunits. As DSP concentration of solutions increased, an increase in the proportion of aggregates of high molecular weight (above 200 kDa) and B-polypeptide was observed. On addition of xanthan (0.025 and 0.05%) to protein solutions (0.5 and 2%), the formation of aggregates of high molecular weight was favoured for both NSP and DSP. In the absence of xanthan, no preferential adsorption of soy polypeptides was observed at the air-water interface of NSP foams. However in DSP foams, there was a preferential adsorption of B-polypeptides. Xanthan present in NSP foams (0.5 or 2%), caused an increase in the proportion of aggregates of high molecular weight at the interface as compared with the composition of solutions used to make the foams. An increase in proportion of AB-polypeptides (for 0.5% NSP and 0.025% xanthan) and B-polypeptides together with polypeptides of molecular weight lower than 14 kDa (for 0.5% NSP and 0.05% xanthan) was also observed at the interface in NSP foams. On the contrary, the presence of xanthan in DSP foams caused a decrease in the proportion of aggregates of high molecular weight and a concomitant increase in B-polypeptide. The B-11S polypeptide predominated the interface of DSP foams probably for its hydrophobicity and basic characteristics. (C) 1999 Elsevier Science B.V. All rights reserved.