Abstract

Desugarization is an important technique in industrial egg processing to maintain the color and shelf life of egg white powder. Its effect on proteolysis of egg white protein is essential in understanding the functionality changes in the obtained hydrolysate. Two desugarization methods, including yeast fermentation and enzyme desugarization using glucose oxidase are commonly employed in industrial scale egg white processing but the suitable method which can improve egg white protein hydrolysates' functionality has not yet been reported. Thus, the present work compares the physicochemical, functional, and surface properties of egg white protein hydrolysates obtained through both the desugarization methods. Alcalase enzyme (2% w/w) was used for enzyme hydrolysis. The degree of hydrolysis of desugared egg white hydrolysate was higher than the non-desugared samples by 34.5%. The desugared samples (especially yeast fermented) had higher foaming and emulsifying ability than non-desugared samples; however, it showed emulsion activity index and surface hydrophobicity. Compared to native protein, the in-vitro trypsin digestibility of desugared hydrolysate samples was significantly (p<0.05) higher. The antioxidant properties increased with hydrolysis, with yeast desugared hydrolysate samples having the highest antioxidant activity (63.8%).

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