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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.

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Protein Purification Protocols for Recombinant Enzymes Produced in Pichia pastoris

  • 实验方案

  • 发表日期：

    2026年

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  • Merve Keser,
  • Mikel Dolz,
  • Javier Viña-Gonzalez,
  • David Gonzalez-Perez,
  • Miguel Alcalde

摘要

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.