Purification of his-tagged proteins using printed monolith adsorption columns

J Chromatogr A. 2024 Sep 27:1733:465216. doi: 10.1016/j.chroma.2024.465216. Epub 2024 Jul 29.

Abstract

Bio-separation is a crucial process in biotechnology and biochemical engineering for separating biological macromolecules, and the field has long relied on bead-based and expanded bed chromatography. Printed monolith adsorption (PMA) is a new alternative to which uses a 3D-printed monolithic structure containing self-supporting, ordered flow channels. PMA allows for direct purification of biological molecules from crude cell lysates and cell cultures, and like the other technologies, can functionalized to specifically target a molecule and enable affinity chromatography. Here we have combined PMA technology with an immobilized metal affinity ligand (iminodiacetic acid) to provide selectivity of binding to polyhistidine-tagged proteins during PMA chromatography. Two different PMA structures were created and tested for both static and dynamic protein-binding capacity. At comparative linear flow rates, the dynamic binding capacity of both columns was ≈3 mg/mL, while static capacity was shown to differentiate based on column voidage. We show that a polyhistidine-tagged protein can be directly purified from crude lysate with comparable results to the available commercial providers of IMAC, and with a substantially reduced purification time.

Keywords: 3D-printed; Chromatography; Crude lysate; GFP; IMAC; PMA; TPMS; printed monolith adsorption.

MeSH terms

  • Adsorption
  • Chromatography, Affinity* / methods
  • Histidine* / chemistry
  • Imino Acids / chemistry
  • Printing, Three-Dimensional
  • Protein Binding
  • Proteins / chemistry
  • Proteins / isolation & purification

Substances

  • Histidine
  • polyhistidine
  • iminodiacetic acid
  • Imino Acids
  • Proteins