Methods for the Production of Recombinant Proteins with Multiple Disulfide Bonds in E. Coli

Background Currently, there is no way to produce complex eukaryotic proteins with multiple disulfide bonds in bacteria. This is because the bacteria cannot normally form the correct disulfide bonds in proteins, since they lack the appropriate enzymatic machinery for this purpose. Such proteins must therefore be produced in mammalian cells at a significant cost.

Invention Description This technology embodies a gram-negative bacterium that has the ability to catalyze the formation and isomerization of disulfide bonds in proteins. Specifically, protein disulfide isomerase is the eukaryotic enzyme employed to mediate the formation of these bonds. It is by way of this enzyme that substantial increases in the production of recombinant proteins in bacteria can be achieved.

Benefits

Spectacular increases in the production of desired recombinant proteins Correctly folded proteins result Low cost

Features

Enzyme utilized can be produced efficiently by bacteria Enzyme is functional in vivo

Market Potential/Applications Since a large number of pharmaceutical proteins have multiple disulfide bonds, many of these can be produced in bacteria by implementing this invention. Further, the total market for proteins whose production could be increased by this invention is estimated at over $2 billion per year.

IP Status One U.S. patent issued: 6,027,888

UT Researcher George Georgiou, Ph.D., Chemical Engineering, The University of Texas at Austin Marc Ostermeier, Ph.D., Chemical Engineering, The University of Texas at Austin

Type of Offer: Licensing



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