The Impact of Six Critical Impurities on Recombinant Protein Recovery and Purification from Plant Hosts

High-Yield Production of Receptor Binding Domain of SARS-CoV-2 Linked to Bacterial Flagellin in Plants Using Self-Replicating Viral Vector pEff

“…Plants along with animal expression systems can perform post-translation modifications while providing safety of products resulting from the absence of pathogens common to plants and animals [9]. Nevertheless, the plant-based expression has also several shortcomings such as (i) low productivity compared to bacterial and mammalian cell cultures [10,11] and (ii) relatively high downstream purification costs, since plant cells need to be lysed to obtain the target protein, while mammalian cells can secrete the target protein to the medium [10,12,13]. Recombinant proteins can be produced in transgenic plants, but their development requires a long time (several months, depending on plant species) and the yield of recombinant protein is usually low (less than 10 µg per gram of fresh biomass) [14].…”

Affinity sedimentation and magnetic separation with plant-made immunosorbent nanoparticles for therapeutic protein purification

“…A semi-quantitative comparison of hIgG binding capacity between the VINs prepared at two levels of purity (data not shown) indicates that there may be a minor reduction in binding capacity between these conditions, likely associated with non-specific blocking by various expected plant host impurities including proteins, salts, polysaccharides, and phenolics (Dixon et al , 2018). However, there was no discernable impact of the solution type (crude extract or purified solution) on reusability of the VINs for an additional cycle of capture and elution.…”