Since its beginnings in the 1970s, recombinant DNA technology has become integral in the production of pharmaceutically important proteins such as blood factors, hormones, growth factors, interferons, interleukins, and vaccines. Recombinant technology was developed in Escherichia coli, and because of its long history of use and ease of manipulation, the bacteria remains a common expression system. However, E. coli is limited in the types of proteins it can express, and production can be hampered by the formation of intracellular inclusion body aggregates which complicate the processes of protein recovery and purification. The non-pathogenic Corynebacterium glutamicum can accumulate amino acids extracellularly and has historically been used for the commercial production of amino acids glutamate and lysine. More recently, C. glutamicum has been developed as an expression system with the ability to secrete properly folded, functionally active proteins into the fermentation broth. Production in C. glutamicum has the same advantages of scalability and ease of culturing as in E. coli, but with more simplified recovery and purification processes…