Inside Back Cover: Enzymatically Active Ultrathin Pepsin Membranes (Angew. Chem. Int. Ed. 20/2015). Issue 20 (27th April 2015)

• Record Type: Journal Article
• Authors: Raaijmakers, Michiel J. T.; Schmidt, Thomas; Barth, Monika; Tutus, Murat; Benes, Nieck E.; Wessling, Matthias
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 20(2015)
• Page Start: 6067
• Page End: 6067
• Publication Date: 2015-04-27
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201503395
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Ultrathin films of cross‐linked enzymes that allow simultaneous enzymatic conversion and selective removal of digestion products are described in the Communication by N. E. Benes, M. Wessling et al. on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 5910 ff.</ext-link> Covalent bonds are formed in an interfacial reaction between the cross‐linker and pepsin, thereby producing thin supported membrane films of potentially unlimited surface area. The high water flux through the membranes transports large proteins to the surface, where they are retained and digested.<graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgjkt780wh" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></p> </abstract>