Polyphenol oxidase depletion in Nicotiana benthamiana enhances recombinant protein purification and preserves native protein integrity
Kaijie Zheng, Farnusch Kaschani, Emma C Watts, Markus Kaiser, Renier A L van der Hoorn · 2026
Read Polyphenol oxidase depletion in Nicotiana benthamiana enhances recombinant protein purification and preserves native protein integrity by Kaijie Zheng, Farnusch Kaschani, Emma C Watts, Markus Kaiser, Renier A L van der Hoorn (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13326509.txt.
Description
Kaijie Zheng and team removed two polyphenol enzymes from Nicotiana benthamiana to improve recombinant protein making. Their 2026 study tackles a real bottleneck. Leaf injection of this plant is widely used for molecular pharming, but enzyme browning and native protein clumping during extraction can damage protein health and cleaning rate. The team made genome-edited lines lacking two oxidase genes and tested them under gentle extraction.
Oxidase-deficient plants browned less and crosslinked less, preserved own proteins at their predicted weights, and showed increased enzyme activity. They also achieved much higher recovery and improved purity of a briefly expressed lab-made protein. The authors identify oxidase-driven oxidation as a major block in that step, and present oxidase depletion as a simple route to cleaner, higher-yield plant-made proteins.
Catalog record
| CREATOR | Kaijie Zheng, Farnusch Kaschani, Emma C Watts, Markus Kaiser, Renier A L van der Hoorn |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 44 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |