Literature DB >> 25779668

Enzymatically active ultrathin pepsin membranes.

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.
© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  biomembranes; interfacial polymerization; membranes; pepsin; proteins

Mesh:

Substances:

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


  2 in total

1.  Flexible single-layer ionic organic-inorganic frameworks towards precise nano-size separation.

Authors:  Liang Yue; Shan Wang; Ding Zhou; Hao Zhang; Bao Li; Lixin Wu
Journal:  Nat Commun       Date:  2016-02-29       Impact factor: 14.919

2.  Amphipathic Janus Membrane with Hierarchical Multiscale Hyperporous Structure for Interfacial Catalysis.

Authors:  Yakai Lin; Yuanyuan Liu; Yicheng Su; Lin Wang; Yuanhui Tang; Tianyin Liu; Liwei Ren; Xiaolin Wang
Journal:  Membranes (Basel)       Date:  2020-07-23
  2 in total

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