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Tillman Gerngross headshot

Tillman U. Gerngross

Professor of Engineering

Professor Gerngross delivers the 29th annual Presidential Faculty Lecture at Dartmouth, discussing his research and career in biotechnology entrepreneurship.


  • BS/MS, Chemical Engineering, Technical University of Vienna, Austria 1989
  • PhD, Molecular Biology, Technical University of Vienna, Austria 1991

Research Interests

Protein engineering; glycoprotein engineering; high cell density fermentation technology; metabolic engineering; protein expression

Selected Publications

  • Gerngross, T.U. It's the problem, stupid! Nature Biotechnology, 30, 742–744 (2012) (Full Text Version)
  • Hamilton, S.R., R.C. Davidson, N. Sethuraman, J.H. Nett, Y. Jiang, S. Rios, P. Bobrowicz, T.A. Stadheim, H. Li, B-K. Choi, D. Hopkins, H. Wischnewski, J. Roser, T. Mitchell, R.R. Strawbridge, J. Hoopes, S. Wildt, T.U. Gerngross. Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins. Science, 313(5792):1441-1443 (2006) (Abstract, Full Text Version)
  • Li, H., N. Sethuraman, T.A. Stadheim, D. Zha, B. Prinz, N. Ballew, P. Bobrowicz, B-K. Choi, W.J. Cook, M. Cukan, N.R. Houston-Cummings, R. Davidson, B. Gong, S.R. Hamilton, J.P. Hoopes, Y. Jiang, N. Kim, R. Mansfield, J.H. Nett, S. Rios, R.l. Strawbridge, S. Wildt, T.U. Gerngross. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nature Biotechnology. 24, 210 - 215 (2006)
  • Hamilton, S.R., H. Li, H. Wischnewski, A. Prasad, J.S. Kerley-Hamilton, T. Mitchell, A.J. Walling, R.C. Davidson, S. Wildt, and T.U. Gerngross. Intact {alpha}-1,2-endomannosidase is a typical type II membrane protein. Glycobiology. 15(6):615-24 (2005)
  • Wildt, S., and T.U. Gerngross. The humanization of N-glycosylation pathways in yeast. Nature Reviews Microbiol. 3(2):119-28 (2005)
  • Gerngross, T.U., Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nature-Biotechnology, 1409 -1414 (2004)
  • Hamilton, S.R., P. Bobrowicz, B. Bobrowicz, H. Li, T. Mitchell, J.H. Nett, S. Rausch, T.A. Stadheim, S. Wildt, H. Wischnewski, and T.U. Gerngross. Production of complex human glycoproteins in yeast. Science, 301, 1244 (2003) (Abstract, Full Text Version)


  • National Academy of Engineering (NAE) Member, 2017


  • ENGS 35: Biotechnology and Biochemical Engineering


  • Medical device comprising polyhydroxyalkanoate having pyrogen removed using oxidizing agent | 8,771,720
  • Method of forming medical devices having pyrogen removed for in vivo application | 8,231,889
  • Medical device comprising polyhydroxyalkanoate having pyrogen removed | 7,906,135
  • ARG1, ARG2, ARG3, HIS1, HIS2, HIS5, HIS6 genes and methods for stable genetic integration | 7,479,389
  • Method for making devices using polyhydroxyalkanoate having pyrogen removed | 7,244,442


Co-Founder and CEO
Co-Founder and Board Chairman
Co-Founder and Board Chairman
Co-Founder and CEO

Research Projects

  • Fermentation processes

    Fermentation processes

    Fermentation processes with high cell densities are important for the production of most bio-therapeutics which is conducted in highly controlled fed-batch processes. Commercial yeast- and E.coli-based fermentation processes often reach cell-densities in excess of 50g/l in fed-batch culture. Our laboratory has developed processes for the high cell density cultivation of Ralstonia eutropha allowing us to reach cell densities of over 150g/l and the expression of recombinant proteins at titers exceeding 10g/l. Much of this is achieved by implementing computer controlled feeding algorithms.

  • Cell-based protein purification systems

    Cell-based protein purification systems

    Cell-based protein purification systems offer advantages over conventional protein purification approaches which rely mostly on chromatographic methods to stepwise enrich for a desired protein of interest. We are developing approaches by which cells are engineered to produce their own affinity matrix to selectively sequester a desired recombinant protein. This allows for the expression and affinity purification of desired proteins in a single host, thereby obviating the need for external chromatographic purification.

  • Cellular engineering of protein expression hosts

    Cellular engineering of protein expression hosts

    Cellular engineering of protein expression hosts provides the ability to modify proteins in a site specific and controlled fashion—something increasingly important for the development of therapeutic proteins. We are developing methods by which cells are genetically engineered to incorporate sugars on a recombinant protein in a site-specific sequence dependent manner. Once a sugar is positioned on a given protein, conventional chemical modification such as PEGlylation can be used to further modify the protein and improve its therapeutic properties.

  • Novel protein expression systems

    Novel protein expression systems

    Novel protein expression systems are being developed based on the soil bacterium Ralstonia eutropha as an alternative to E.coli-based protein expression. This bacterial host can be grown to cell densities in excess of 150g/l in ultra high cell density culture and allow for the recovery of proteins that are prone to inclusion body formation in E.coli. Specific model proteins have been expressed at levels 100 fold higher than in E.coli thereby providing the impetus for further developing Ralstonia eutropha for the production of therapeutic proteins including monoclonal antibodies and peptides.

  • Humanization of glycosylation in yeast

    Humanization of glycosylation in yeast

    Humanization of glycosylation in yeast enables the use of yeast-based protein expression systems which offer inherent advantages over conventional mammalian cell culture. By engineering yeast-based systems to perform human-like glycosylation fully-humanized therapeutic proteins can be produced in these glyco-engineered hosts.

  • Glyco-engineering of proteins

    Glyco-engineering of proteins

    Glyco-engineering of proteins is being developed as a method to control the composition of glycans on glycoproteins. Such methods are of great importance in the biopharmaceutical industry because glyocoproteins constitute over 60% of all approved therapeutic proteins; and the therapeutic properties of many glycoproteins strongly depend on the composition of their glycans.


The Scientist
Remaking a Classic
Sep 03, 2013
Mar 07, 2011
Carbohydrate Advances
Mar 07, 2011