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Recombinant Porcine Trypsin

Polymun has proprietary yeast recombinant porcine trypsinogen that is autocatalytically activated to the active enzyme. This recombinantly manufactured enzyme can replace trypsin derived from animal origin.

 

Recombinant porcine trypsin has defined activity (e.g. free of chymotrypsin or elastase activity without inhibitor treatment) and is free of animal tissue derived contaminants. Recombinant trypsin is a valuable tool to improve both quality and safety in mammalian cell culture, cell based therapy applications as well as for drug manufacturing processes using trypsin as process enzyme (e.g. insulin production).

Polymun has signed a license agreement with Richcore Enzymes Pvt Ltd (Bangalore, India) for the recombinant porcine trypsin technology. Richcore is manufacturing this recombinant porcine trypsin in large scale kilogram quantities for use in GMP processes.

You can order rpTrypsin as research reagent.

PATENTS

Method for the manufacture of recombinant trypsin
granted by: EP 1 250 442; 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