In vitro gastric and duodenal digestibility of protein isolates from quail egg

Abstract

We isolate the protein by its isoelectric point, quantify, characterize and subject them to in vitro digestion studies. Taking into account 4 types of samples to check as time passes the proteins are preserved or lost. Eggs collected at 12 hours after laying showed that they had a protein content of 87.22%, eggs collected at 24 hours after laying 87.80%, eggs collected at 48 hours after laying 86.26 % and eggs collected at 72 hours after laying 90.28% showing that the quail egg has a high protein value compared to the chicken egg. In the protein characterization through SDS-PAGE electrophoresis, we were able to evaluate the types of protein that this product has taking into account that lysozyme and ovomucine were isolated, so in this study their bands are almost non-existent. Ovotransferrin (77kDa), Avidin 65-69ka), Ovoglobulin G3 (50-55 kDa), Ovalbumin (39 kDa) and Lysozyme fractions (12kDa), observed in all the samples studied, therefore these proteins are conserved if they are not subjected to Sudden temperature changes greater than 50 ° C and less than 25 ° C. Therefore, for the simulation of the gastrointestinal process in vitro enzymes such as pepsin, pancreatin and bile salts were used, preparing them at different pHs and simulating the stomach of a person suffering from gastrointestinal problems pH 1.2 stomach of a healthy adult person pH2, 0 and non-infant child pH3,2; We determined that quail egg proteins are fully digested at pH 1.2 and at pH 3.2, ovotranferrin and ovalbumin protein have problems for their total digestion