Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 5910-5914 |
| Journal | Angewandte Chemie (international edition) |
| Volume | 54 |
| Issue number | 20 |
| DOIs | |
| Publication status | Published - 2015 |
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Enzymatically Active Ultrathin Pepsin Membranes. / Raaijmakers, Michiel; Schmidt, Thomas; Barth, Monika; Tutus, Murat; Benes, Nieck E.; Wessling, Matthias.
In: Angewandte Chemie (international edition), Vol. 54, No. 20, 2015, p. 5910-5914.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Enzymatically Active Ultrathin Pepsin Membranes
AU - Raaijmakers, Michiel
AU - Schmidt, Thomas
AU - Barth, Monika
AU - Tutus, Murat
AU - Benes, Nieck E.
AU - Wessling, Matthias
PY - 2015
Y1 - 2015
N2 - 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.
AB - 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.
U2 - 10.1002/anie.201411263
DO - 10.1002/anie.201411263
M3 - Article
VL - 54
SP - 5910
EP - 5914
JO - Angewandte Chemie (international edition)
JF - Angewandte Chemie (international edition)
SN - 1433-7851
IS - 20
ER -