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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Protein Purification Protocols for Recombinant Enzymes Produced in Pichia pastoris
Merve Keser1, Mikel Dolz2, Javier Viña-Gonzalez2
1Department of Biocatalysis, Institute of Catalysis, CSIC, Madrid, Spain.
Abstract:
Komagataella phaffii is usually a microbial host of choice for eukaryotic enzyme expression and overproduction in fed-batch bioreactors. The design of a fast and reliable protein purification protocol is crucial to perform a detailed biochemical characterization of the recombinant enzyme. Here, we provide standardized methods for ion exchange chromatography (IEC) and immobilized metal affinity chromatography (IMAC) in the ÄKTA system that are broadly used for the purification of heterologous enzymes produced in K. phaffii.

