Isolation, Purification and Antimicrobial Efficacy of Ovotransferrin from Eggs of Broiler, Domestic and Quail

Abstract

Ovotransferrin is one of the major egg white proteins that have antimicrobial activity as well as iron binding capability. The objective of this study was to develop a simple and easy method to separate ovotransferrin using organic solvents. The purity of the ovotransferrin was determined using SDS-PAGE, the isolated protein was further studied for the assessment of interaction between food borne pathogens and the isolated Otrf by protein-protein molecular docking. However, this method is simpler and more cost effective than the previous method. The isolated ovotransferrin can be used as is or after modifications for various applications such as antimicrobial treatments. Recently, the iron chelating activity of Otrf has been exposed to upsurge the stimulus by an inhibitor of AMPc ß-lactamase of some antibiotics which are efficient against most ß-lactamase-producing bacteria. Cefiderocol is a siderophore cephalosporin antibiotic that has recently been developed to combat a variety of bacterial pathogens, including ?-lactam and carbapenem-resistant organisms. OtrF is currently recommended for use in conjunction with antibiotics unless further studies increase the effectiveness of OtrF. These studies highlight the separation, purification of potential diversity in antimicrobial efficacy of Otrf.