Alternative application of an affinity purification tag: hexahistidines in ester hydrolysis

L. Schoonen, K.S. van Esterik, C. Zhang, R.V. Ulijn, R.J.M. Nolte, J.C.M. van Hest

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)
125 Downloads (Pure)


Hexahistidines are very common tags used in the affinity chromatography purification of recombinant proteins. Although these tags are solely applied for their metal-binding properties, we found that they are also able to perform ester hydrolysis when attached to a protein. For instance, green fluorescent protein (GFP) and the cowpea chlorotic mottle virus (CCMV) are able to perform catalysis after introduction of the His-tag. By attaching a His-tag to an enzyme, a dual-functional catalyst was created, that can perform a two-step cascade reaction. These findings show that the catalytic properties of the hexahistidine tag should be taken into consideration when choosing a suitable protein purification tag
Original languageEnglish
Article number14772
Number of pages9
JournalScientific Reports
Issue number1
Publication statusPublished - 1 Dec 2017


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