PRODUCTION OF RECOMBINANT AVIDIN IN ESCHERICHIA-COLI

A recombinant avidin (re-Avd), containing amino acids (aa) 1-123 of th e native chicken egg-white Avd, was produced in Escherichia coli. When cells were grown at 37 degrees C production was over 1 mu g/ml, due t o altering the codon preference of the first ten codons. The re-Avd wa s recovered as a soluble protein from cells grown at 25 or 30 degrees C, whereas at 37 degrees C it was mostly insoluble in inclusion bodies . Our results indicated that, despite the potentially harmful biotin-b inding activity of Avd, it is possible to produce biologically active Avd in E. coli which then can easily be purified by affinity chromatog raphy on a biotin column in a single step.