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<p>A recombinant modified human transferrin (N413D and N611D) was produced by the <i>Pichia pastoris</i> strain pPIC9pGAPZalpha-short_hTFNG (Yst-TFNG2). A multi-step protocol for isolation and purification of recombinant transferrin was developed achieving the target protein yield of 70.29% and a purity of at least 95%. Structural correspondence of the recombinant transferrin to the natural protein was confirmed by mass spectrometry and circular dichroism analysis. Functional analysis demonstrated the protein’s ability to bind and release iron ions, as well as support the proliferation of eukaryotic cells.</p>

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Isolation, Purification, and Structural-Functional Analysis of Recombinant Human Transferrin Produced by the Methylotrophic Yeast Strain Pichia pastoris

  • 期刊论文

  • 发表日期：

    2025年9月1日

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  • R. Yu. Popov,
  • E. D. Nikolskaya,
  • T. K. Aliev,
  • N. N. Kostin,
  • T. V. Bobik,
  • A. G. Gabibov

摘要

A recombinant modified human transferrin (N413D and N611D) was produced by the Pichia pastoris strain pPIC9pGAPZalpha-short_hTFNG (Yst-TFNG2). A multi-step protocol for isolation and purification of recombinant transferrin was developed achieving the target protein yield of 70.29% and a purity of at least 95%. Structural correspondence of the recombinant transferrin to the natural protein was confirmed by mass spectrometry and circular dichroism analysis. Functional analysis demonstrated the protein’s ability to bind and release iron ions, as well as support the proliferation of eukaryotic cells.