Abstract

The aim of the research was to use low-mineral egg white albumin isolate to obtain aerated calcium ion-induced gels and to investigate their aptitude as matrices for active ingredients release. Aerated gels were prepared by adding calcium ions to pre-heated protein dispersions with simultaneous aeration. 20 mM calcium concentration was an optimal concentration at which the maximum viscosity and hardness of the gels were found. For higher concentrations of calcium ions (25–30 mM), aerated gels were characterized by lower values of the moduli and tangent of the phase angle was larger for aerated gels which indicated more viscous character than that of non-aerated gels. Increased ions concentration causes higher aggregation of protein matrix and less smooth microstructure of the interface between the gel and air. An increase in calcium concentration from 5 to 30 mM caused an increase in an average bubble size. The release of calcium ions from aerated gels was measured in an artificial stomach. It occurred by Fickian diffusion through the swelling matrix and it was faster for the gels with higher concentration of calcium. An increase in calcium concentration caused an increase in surface roughness of the aerated gels. There were linear correlations between the quadratic mean of the surface roughness and “n” coefficient from the Ritger and Peppas equation and between the maximum roughness size and “n”. The increased calcium concentration made the gel microstructure more particulate and the surface rougher, which enabled faster proteolysis of the gel in an artificial stomach and faster diffusion of calcium ions.

Highlights

  • Proteins of animal origin should be the main source of amino acids in human diet

  • Low-mineral egg white albumin isolate is a good material for ions-induced gelation

  • There is an optimal concentration of calcium ions at which the aerated gels are the strongest

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Summary

Introduction

Proteins of animal origin should be the main source of amino acids in human diet. Chicken egg protein is treated as a reference protein. Egg white has a protein content of about 11 % and comprises about 58 % of the entire egg mass [1]. The main proteins of egg white are ovalbumin, ovotransferrin, ovomucoid, globulins and lysozyme. Egg white protein has excellent functional properties and among them, the most important are: gelation, foaming and emulsification. Along with high nutritional value, it is a very important substrate for food industry

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