Related Experiment Video
Updated: Jul 12, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 26, 2010
Expression and characterization of human interferon-beta1 in the methylotrophic yeast Pichia pastoris
Natasa Skoko1, Barbara Argamante, Natasa Kovacević Grujicić
1Institute of Molecular Genetics and Genetic Engineering, Vojvode Stepe 444a, 11001 Belgrade, Serbia and Montenegro. nataskoko@yahoo.it
Abstract:
We describe the heterologous expression of a human interferon-beta1 in the methylotrophic yeast Pichia pastoris. Biologically active recombinant human interferon-beta1 (rHuIFN-beta1) was secreted from shake-flask-grown P. pastoris cells into the medium using the Saccharomyces cerevisiae alpha-mating factor prepro-leader sequence at the level of (1-3) x 10(5) i.u. (international units)/ml (6-12 mg/litre). An rHuIFN-beta1 with an N-terminal sequence identical with that of native HuIFN-beta1 was purified and the specific activity was determined (2-3 x 10(7) i.u./mg). It was found that the secreted recombinant protein was partially N-glycosylated.
Related Concept Videos
Yeast Signaling
Bioreactor Controls-III
Production of Pharmaceuticals
Inhibitors of Viral Protein Synthesis

