STRUCTURE-FORMING PROPERTIES OF SAPONIN-CONTAININGFOOD SYSTEMS

CPSZCA

Abstract

The problem of studying saponin-containing raw materials in food systems is relevant, it is increasingly used in food technologies, especially with foam and emulsion structures. The paper considers the surface active properties of saponins with egg albumin, modeling a variety of food systems with their participation. Triterpene saponins (from Merck and saponin from horse chestnuts) were selected for the study, which have oleanolic acid as an aglycone, which causes antimicrobial, anticancer, hepatoprotective, antioxidant, lipid-lowering and other effects.

The experiment included an assessment of the properties of solutions of two saponins and egg albumin depending on their concentration from the standpoint of the structural and mechanical stability factor, and then the effect of egg albumin on saponin solutions according to the same indicators. The solutions were characterized by surface tension, the strength of the interfacial adsorption layer, active acidity and emulsifying ability. To obtain results in a close range of values, the concentration of the studied egg albumin solutions (0.1-1.0%) is an order of magnitude higher than the concentration of saponin solutions (0.01-0.1%), which is due to the very high surface activity of the latter. The effect of albumin on 0.05% saponin solutions was determined at concentrations of 0.05-0.5%.

It has been established that, depending on the active acidity of solutions, there are two multidirectional trends in the formation of egg albumin associates with saponins. The role of individual substances in the stabilization of emulsions and foams is shifting in one direction or another due to the possibility of the formation of saponin-protein associates and their colloidal chemical properties. When saponin-protein associates are formed, the ability of protein macromolecules to structure in MAC decreases, but at the same time, due to the unique structure of the associates, the possibilities of significant lyophilization of the aqueous solution-oil interface open up.