| Literature DB >> 25779668 |
Michiel J T Raaijmakers1, Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E Benes, Matthias Wessling.
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.Entities:
Keywords: biomembranes; interfacial polymerization; membranes; pepsin; proteins
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Year: 2015 PMID: 25779668 DOI: 10.1002/anie.201411263
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336