Bioseparation of recombinant proteins from plant extract with hydrophobin fusion technology

Jussi J. Joensuu*, Andrew J. Conley, Markus B. Linder, Rima Menassa

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterScientificpeer-review

15 Citations (Scopus)


Two main hurdles hinder the widespread acceptance of plants as a preferred protein expression platform: low accumulation levels and expensive chromatographic purification methods. Fusion of proteins of interest to fungal hydrophobins has provided a tool to address both accumulation and purification issues. In this method, we describe the one-step purification of a GFP-HFBI fusion from crude plant extract using an aqueous two-phase system (ATPS). ATPS can be carried out in a very short time frame, yields relatively pure protein with very few contaminants, and does not require any chromatographic column steps. This purification system takes advantage of the affinity of hydrophobins to the micellar phase of widely available nonionic surfactants, such as Triton X-114, and can be easily scaled up for industrial-scale protein purification.

Original languageEnglish
Title of host publicationRecombinant Gene Expression
Subtitle of host publicationReviews and Protocols, Third Edition
EditorsArgelia Lorence
Number of pages8
Publication statusPublished - 23 Jan 2012
MoE publication typeA3 Part of a book or another research book

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Aqueous two-phase system
  • ATPS
  • HFBI
  • Hydrophobin
  • Molecular farming
  • Protein fusion
  • Protein purification


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