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Updated: Jun 3, 2026

Apoplast-Extraction Based Method to Improve the Purity of Plant Produced Recombinant Protein
Published on: July 5, 2024
Biopharmaceuticals from plants: a multitude of options for posttranslational modifications
1Darmstadt University of Technology, Department of Botany, 64287 Darmstadt, Germany. warzecha@bio.tu-darmstadt.de
Abstract:
In 1982 the first recombinant therapeutic, human insulin, was introduced into the market and started a new branch of pharmaceutical development, manufacture, and therapy options. To date, more than 130 recombinant protein therapeutics have been approved by the US Food and Drug Administration (FDA) and many more are being developed world wide. With the increasing number of protein therapeutics the number of potential production organisms is also expanding, and posttranslational modification of proteins has become a topic of special focus. One major difference between small-molecule drugs and protein therapeutics is that the latter are reliant on a host organism for their production and this can have a large influence on the final structure and can ultimately affect the pharmacokinetics, immunogenicity, and the function of the protein depending on the production process. Plants can be efficiently used as production systems for recombinant proteins thereby offering a variety of options for transgene targeting and modification. This review is intended to give an overview about the potential of plants to serve as a production system for therapeutic and prophylactic biopharmaceuticals with respect to posttranslational modifications.
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