Enzymatically Active Ultrathin Pepsin Membranes

Michiel Raaijmakers, Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E. Benes, Matthias Wessling

Research output: Contribution to journalArticleAcademicpeer-review

14 Citations (Scopus)

Abstract

Enzymatically active proteins enable efficient and specific cleavage reactions of peptide bonds. Covalent coupling of the enzymes permits immobilization, which in turn reduces autolysis-induced deactivation. Ultrathin pepsin membranes were prepared by facile interfacial polycondensation of pepsin and trimesoyl chloride. The pepsin membrane allows for simultaneous enzymatic conversion and selective removal of digestion products. The large water fluxes through the membrane expedite the transport of large molecules through the pepsin layers. The presented method enables the large-scale production of ultrathin, cross-linked, enzymatically active membranes.
Original languageEnglish
Pages (from-to)5910-5914
JournalAngewandte Chemie (international edition)
Volume54
Issue number20
DOIs
Publication statusPublished - 2015

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  • Cite this

    Raaijmakers, M., Schmidt, T., Barth, M., Tutus, M., Benes, N. E., & Wessling, M. (2015). Enzymatically Active Ultrathin Pepsin Membranes. Angewandte Chemie (international edition), 54(20), 5910-5914. https://doi.org/10.1002/anie.201411263