Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 30, Pages 8585-8589Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201602353
Keywords
affinity separation; bioconjugation; cyclodextrins; enzyme recycling; protein modification
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Funding
- Energy Biosciences Institute at UC Berkeley
- NSF [CHE-1413666]
- Villum Kann Rasmussen Foundation
- National Defense Science & Engineering Graduate (NDSEG) Fellowship
- Berkeley Fellowship for Graduate Study
- Berkeley Chemical Biology Graduate Program (National Research Service Award Training grant) [1 T32 GMO66698]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1413666] Funding Source: National Science Foundation
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Enzyme-mediated protein modification often requires large amounts of biocatalyst, adding significant costs to the process and limiting industrial applications. Herein, we demonstrate a scalable and straightforward strategy for the efficient capture and recycling of enzymes using a small-molecule affinity tag. A proline variant of an evolved sortase A (SrtA 7M) was N-terminally labeled with lithocholic acid (LA)-an inexpensive bile acid that exhibits strong binding to beta-cyclodextrin (beta CD). Capture and recycling of the LA-Pro-SrtA 7M conjugate was achieved using beta CD-modified sepharose resin. The LA-Pro-SrtA 7M conjugate retained full enzymatic activity, even after multiple rounds of recycling.
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