Abstract
The present study investigated proteolysis combined with heat treatment to make hen Egg White (EW) an efficient emulsifier. EW was hydrolyzed by protease (Thermoase®) at various Enzyme Concentrations (EC) (w/w, 0.1%, 0.2%, 0.4%, 0.8%), followed by heating at 90°C for 8 min. Results showed that optimal emulsifying ability and stability, determined by measurement of emulsion turbidity, were obtained when EC was 0.4%, followed by heat treatment at 90°C. The hydrolysate thus prepared had higher emulsifying ability and stability than either native egg white (nEW) or small molecular weight EW peptides (Runpep®), close to the properties of Egg Yolk (EY) which was a reference as a food emulsifier. Surface hydrophobicity (H0) was found to be linearly related to the emulsifying activity and stability of hydrolyzed egg white proteins.
Highlights
Egg White (EW) is a significant protein source of dietary protein, accounting for about 58% of the entire mass of an egg, with a protein content of about 10% (Abeyrathne et al, 2013, Kovacs-Nolan et al, 2005)
The Emulsifying Stability (ES) of hydrolysates of lupin protein and α-conglutin decreased relative to the native proteins, lupin protein hydrolysates were still thought to be potential to be used as ingredients in emulsion-based food formulations such as salad dressing and mayonnaise
HEW and water were homogenized with a weight ratio of 3:2:1 by a mechanical dispenser (Polytron PT-MR2100, Switzerland) at 25,000 rpm for 1 min, 200 μL of emulsion was pipetted from the bottom of the container immediately (T0) and 2 h (T2h) after homogenization
Summary
Egg White (EW) is a significant protein source of dietary protein, accounting for about 58% of the entire mass of an egg, with a protein content of about 10% (Abeyrathne et al, 2013, Kovacs-Nolan et al, 2005) It is known as a desirable ingredient for many foods such as bakery goods, meringues and meat products in which it is mainly used because of its excellent gelling and foaming properties (Alamprese et al, 2012). Proteolysis has been suggested as an efficient way to improve functional properties by Lqari et al (2005) These authors showed that lupin protein and α-conglutin hydrolyzed using alkaline protease (alcalase) had better Emulsifying Activity (EA) than native lupin protein and α-conglutin, respectively. A relationship between H0 versus EA and H0 versus ES was attempted to be established
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