Modificación de la actividad enzimática de Lisozima de clara de huevo de gallina, por hidrólisis gástrica y tratamiento térmico (microondas).

Abstract

The lysozyme is a chicken egg protein may represent about 3.5 percent of them. It is also a source of essential amino acids for human consumption, which has led to a thorough study, mainly from its protein. In this study we worked with lysozyme and purified commercial egg in the laboratory of functional foods BIPROPEPTI. These two samples were modiffied in their enzymatic activity gastric hydrolysis and heat treatment with microwaves. It was possible to purify the lysozyme from chicken egg by using protein flash chromatography (FPLC) and 1 M NaCl precipitation showed enzymatic activity. In addition, gastric hydrolysis of lysozyme from chicken egg at pH 1.2 showed that hydrolysis was complete. Also, gastric hydrolysates of egg white lysozyme commercial hen at pH 1.2; 2.0 and 3.2 showed enzymatic activity of 23, 47 and 42 percent respectively. Similarly, hydrolysates of egg white lysozyme purified hen enzyme activity values presented as 20, 35 and 48 percent at pH 1.2; 2.0 and 3.2 respectively. The lysozyme of egg white and purified commercial hen subjected to heating (microwave) had enzyme activities of 99, 92, 85 and 73 percent in commercial lysozyme respectively. Also, the purified lysozyme introduced enzymatic activities of 99, 97, 96 and 95 percent. The hydrolyzate of both commercial and purified lysozyme were able to inhibit lipid peroxidation in zebrafish larvae.