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Background The use of Escherichia coli for the production of recombinant proteins is an established strategy to obtain biotechnological tools. However, the recombinant protein expression is dependent on temperature, bacterial culture time, induction period, nutrients, plasmid characteristics, and insert itself. Thus, the aim of this study was optimize the expression of recombinant gE protein (rgE) from Bovine Herpesvirus types 1 and 5.

Culture optimization of Escherichia coli for expression of gE proteinfrombovine herpesvirus 1 and 5