Combined effects of NaOH, NaCl, and heat on the characteristics of ovalbumin gel and the exploration of the mechanism of transparent gel formation

Salted preserved eggs are made using poultry eggs under the combined action of NaOH, NaCl, and heat. To elucidate the main basis and mechanism of the formation of salted preserved egg white, the effects of NaOH (0.5–2.5%), NaCl (0–1.2%), and heat (72–100 °C) on the properties of ovalbumin (the most abundant protein in poultry egg whites) gel were studied. With increasing NaOH addition, the pH and the absolute value of zeta potential (TAV-ZP) increased, the opacity and Hunter whiteness decreased, and the relaxation time (T2) initially decreased and then increased. With increasing NaCl addition and heating temperature, the pH and TAV-ZP decreased, the opacity and Hunter whiteness increased, and T2 decreased first and then increased. In addition, the hardness and cohesiveness of the ovalbumin gel were greatly modified by NaOH, NaCl, and heat. NaOH contributed to the formation of the gel network structure. In addition, the surface hydrophobicity (H0) analysis result indicated that the tertiary structure of the ovalbumin had changed during the formation of the ovalbumin gel. The correlation analysis results showed that electrostatic repulsion played a vital role in the formation of the transparent ovalbumin gel, and the transparent ovalbumin gel possessed the following characteristics: low aggregation degree, high cross-linking degree, high immobilized water content, gel network structure, and the fully unfolded structure of ovalbumin molecules. In general, the ovalbumin formed a unique gel under the combined action of NaOH, NaCl, and heat. This study could provide theoretical guidance for the processing and control of salted preserved eggs and a reference for highly transparent egg white gel products.