Paper Title
Expression and Purification of Recombinant Bacteriocin lac101 in Escherichia coli Stain BL21 (DE3) pLysS Using Bioinformatics Database

Due to the overuse of antibiotics at present it results in infection from microorganisms with a higher rate and tendency thus causing a campaign to resist the use of more antibiotics. This include the development of new methods to replace the antibiotics alone. Therefore, we study the expression of peptide lac010, its purification and antimicrobial properties in the Escherichia coli system. By gene design and the addition of His6TAG gene for purification via cloning into the vector pET25b (+) for expression in E.coli bacteria BL21 (DE3)pLysS, peptide lac010 was designed to be 13.43 kDa. Based on the results of the analysis using the SDS-PAGE gel technique, it can be produced in the form of soluble peptides and in a form that can work. After induction at 16 degrees Celsius, which can be an antimicrobial agent in the pathogenesis by testing against Gram-negative bacteria (Vibrio parahaemolyticus) Keywords - Bacteriocin, Bioinformatics Database, Inhibition, Foodborne pathogens