Enzymatically Active Ultrathin Pepsin Membranes

Michiel Raaijmakers, Thomas Schmidt, Monika Barth, Murat Tutus, Nieck E. Benes, Matthias Wessling

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)5910-5914
JournalAngewandte Chemie (international edition)
Volume54
Issue number20
DOIs
Publication statusPublished - 2015

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Pepsin A
Membranes
Interfacial polycondensation
Enzyme immobilization
Peptides
Chlorides
Fluxes
Proteins
Molecules
Water

Cite this

Raaijmakers, Michiel ; Schmidt, Thomas ; Barth, Monika ; Tutus, Murat ; Benes, Nieck E. ; Wessling, Matthias. / Enzymatically Active Ultrathin Pepsin Membranes. In: Angewandte Chemie (international edition). 2015 ; Vol. 54, No. 20. pp. 5910-5914.
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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 journalArticleAcademicpeer-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)

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