title: Enzymatically active ultrathin pepsin membranes.
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.
authors.affiliation: Inorganic Membranes, University of Twente, Faculty of Science and Technology, MESA+ Institute for Nanotechnology, P.O. Box 217, 7500 AE Enschede (The Netherlands).
authors.forename: Michiel J T
authors.initials: MJ
authors.lastname: Raaijmakers
authors.forename: Thomas
authors.initials: T
authors.lastname: Schmidt
authors.forename: Monika
authors.initials: M
authors.lastname: Barth
authors.forename: Murat
authors.initials: M
authors.lastname: Tutus
authors.forename: Nieck E
authors.initials: NE
authors.lastname: Benes
authors.forename: Matthias
authors.initials: M
authors.lastname: Wessling
mesh_terms: D004789:Enzyme Activation; D010434:Pepsin A / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D010434:Pepsin A
keywords: biomembranes; interfacial polymerization; membranes; pepsin; proteins