Refolding of Biopharmaceuticals by FOLDTEC: A Case Study on Recombinant Thrombin

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This webcast features: Dr. Andreas Anton, Director Bioprocess Development and Dr. Sebastian Schuck, Senior Manager Business Development, Wacker Biotech

While WACKER’s own technology ESETEC^® has proven highly efficient in producing soluble proteins and antibody fragments via secretion, poorly soluble substances form aggregated inclusion bodies within the cell, which contain incorrectly and/or incompletely folded target proteins. Recently Wacker Biotech introduced FOLDTEC^®, its novel refolding technology for bioengineered pharmaceutical proteins. With this new technology, biopharmaceuticals that tend to aggregate can be efficiently produced in their soluble-active form in high yields. The proprietary process utilizes specifically developed and optimized bacterial strains and a patented, antibiotic-free expression system. Furthermore, Wacker Biotech offers years of experience in the iterative screening of optimum refolding conditions in order to convert the insoluble target-protein aggregates into the biologically active form.

The potential of this new technology will be demonstrated in a recent case study on recombinant expression and in vitro refolding of thrombin, a key protease in the coagulation cascade. Thrombin is a difficult-to-manufacture enzyme used in surgery and other medical applications to control bleeding. Thanks to the FOLDTEC^® toolbox, space/time yields have been increased successfully by 20-fold!