Surface Adsorption Properties of Peptides Produced by Non-optimum pH Pepsinolysis of Proteins: A Combined Experimental and Self-Consistent-Field Calculation Study

Hypothesis Partial hydrolysis of large molecular weight (Mw), highly aggregated plant proteins is frequently used to improve their solubility. However, if this hydrolysis is extensive, random or nonselective, it is unlikely to improve functional properties such as surface activity, emulsion, or foam-stabilising capacity.

Experiments and simulation Soy protein isolate (SPI) was hydrolysed by pepsin under optimal (pH 2.1) and non-optimal (pH 4.7) conditions. The surface activity and emulsion stabilising capacity of the resultant peptides were measured and compared. The colloidal interactions between a pair of emulsion droplets were modelled via Self-Consistent-Field Calculations (SCFC).

Findings Hydrolysis at pH 2.1 and 4.7 resulted in a considerable increase in measured surface activity compared to the native (non-hydrolysed) SPI, but the hydrolysate from pH 2.1 was not as good an emulsion stabiliser as the hydrolysate (particularly the fraction Mw > 10 kDa) at pH 4.7. Furthermore, peptide analysis of the latter suggested it was dominated by a fragment of one of the major soy proteins β-conglycinin, with Mw ≈ 25 kDa. SCFC calculations confirmed that interactions mediated by adsorbed layers of this peptide point to it being an excellent emulsion stabiliser.