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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Expression and aggregation of recombinant human consensus interferon-alpha mutant by Pichia pastoris
Yuyou Hao1, Ju Chu, Yonghong Wang
1State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, PR China.
Abstract:
A recombinant human consensus interferon-alpha mutant (cIFN) was expressed in Pichia pastoris. The maximum dry cell weight, cIFN concentration and antiviral activity were 160 g l(-1), 1.24 g l(-1) and 4.1 x 10(7) IU ml(-1), respec tively. The cIFN secreted into the medium was in the form of aggregates dominantly by non-covalent interaction and partially by disulphide bond. When the fermentation supernatant was disaggregated with 6 M guanidine hydrochloride, the antiviral activity of cIFN achieved 2.2 x 10(8) IU ml(-1).

