Emulsifying and emulsion stabilizing properties of soy protein hydrolysates, covalently bonded to polysaccharides: The impact of enzyme choice and the degree of hydrolysis

Emulsifying and emulsion stabilizing properties of fragments, derived from vegetable proteins (soy protein isolate) covalently linked to maltodextrin have been studied. The dual role the degree hydrolysis (DH) in improving solubility soy isolate (SPI) on one hand difficulties linking hydrolysates polysaccharide other, highlighted. findings compared results obtained for whey (WPI) undergoing same enzymatic fragmentation subsequent Maillard reaction. All experiments were conducted with two very different enzymes. Trypsin is rather selective peptide bonds it cleaves, while alcalase less specific. At DH, actions these enzymes behaviour resulting conjugates found be broadly similar hydrolysates. In contrast, trypsin generated fragments showed distinctly superior emulsifying than those produced by alcalase. These differences related physical form SPI existing as small colloidal aggregates solution at time hydrolysis, whereas WPI was present a molecularly well-dissolved protein. It shown that, realizing best stabiliser, improved result higher level offset deterioration surface functionality polypeptides due further fragmentation. This leads an optimum value DH synthesising most suitable based emulsifiers. For commercial used this study around 8%. • Solubility crucial achieving desired conjugates. solubility, Excessive detrimental or them. Competing needs adequate properties, hydrolysis. Optimal depends state solution.