Recombinant Human and Porcine Trypsin

Polymun has proprietary yeast recombinant human and porcine trypsinogen that is autocatalytically activated to the active enzyme. These products are intended to replace trypsin derived from animal origin.

Recombinant human trypsin and recombinant porcine trypsin have defined activity (e.g. free of chymotrypsin or elastase activity without inhibitor treatment) and are free of animal tissue derived contaminants. They are valuable tools to improve both quality and safety in various cell culture applications, such as cell based therapy applications and industrial expression systems using cell culture hosts, as well as for manufacturing drugs and/or direct application as a drug.

Polymun is currently establishing GMP-conform manufacturing processes. You can order rhTrypsin and rpTrypsin as research reagents.

Polymun is open to strategic and/or financial partnerships for commercial development.

Patents:

Method for the manufacture of recombinant trypsin
granted by: EP 1 250 442 (AT BE CH/LI DE FR GB IE IT NL SE); SG 90540; US 7,351,549

Publications:

Gasser B, Sauer M, Maurer M, Stadlmayr G, Mattanovich D (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507

Hohenblum H, Gasser B, Maurer M, Borth N, Mattanovich D (2004) Effects of gene dosage, promoters and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol Bioeng 85:367-75

Hohenblum H, Vorauer-Uhl K, Katinger H, Mattanovich D (2004) Bacterial expression and refolding of human trypsinogen. J Biotechnol 109:3-11

Hohenblum H, Borth N, Mattanovich D (2003) Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry. J Biotechnol 102:281-90

Hohenblum H, Naschberger S, Weik R, Katinger H, Mattanovich D (2001) Production of recombinant human trypsinogen in Escherichia coli and Pichia pastoris. A comparison of expression systems. In: Production of recombinant proteins with prokaryotic and eukaryotic cells. Eds.: Merten OW, Mattanovich D, Cole J, Lang C, Larsson G, Neubauer P, Porro D, Postma P, Teixeira de Mattos J, Kluwer Academic Publ, pp. 339-46