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

Introduction

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

U.S. Patent Issued: 6,027,888

UT Researcher

George Georgiou, Ph.D., Department of Chemical Engineering, The University of Texas at Austin

For further information please contact

University of Texas,
Austin, USA
Website : www.otc.utexas.edu