Chemical Permeabilization of Cells for Intracellular Product Release

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Abstract
Recent advances in recombinant DNA technology have made it possible to produce a large array of valuable proteins using a wide variety of host cell systems. Unfortunately, the problem of including microorganisms to secrete foreign proteins they have been programmed to synthesize continues to defy systematic solution. This problem is particularly pronounced with the two most common microbial hosts for recombinant DNA, Escherichia coli and yeast. Normal E. coli cells do not secrete any native proteins to the extracellular medium, although some leaky mutants have been isolated. In the case of yeast, attempts at genetically engineering secretion have met with only mixed success, due to a lack of understanding of the factors determining the final subcellular locations of yeast proteins. Furthermore, with E. coli, final product recovery is often complicated by the fact that many recombinant proteins aggregate into insoluble inclusion bodies.

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