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Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique

Published on: July 19, 2019

Enzymatically active ultrathin pepsin membranes.

Michiel J T Raaijmakers¹, Thomas Schmidt, Monika Barth

¹Inorganic Membranes, University of Twente, Faculty of Science and Technology, MESA+ Institute for Nanotechnology, P.O. Box 217, 7500 AE Enschede (The Netherlands).

Angewandte Chemie (International Ed. in English)

|March 18, 2015

Summary

Ultrathin pepsin membranes were created for efficient protein digestion. This immobilization method enhances enzyme stability and allows for simultaneous enzymatic conversion and product removal.

Keywords:

biomembranes interfacial polymerization membranes pepsin proteins

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Area of Science:

Biochemistry
Materials Science
Chemical Engineering

Background:

Enzymatically active proteins, like pepsin, are crucial for specific peptide bond cleavage.
Enzyme immobilization is key to preventing autolysis-induced deactivation and enhancing stability.
Developing efficient methods for enzyme-based bioconversion and separation is an ongoing challenge.

Purpose of the Study:

To develop a method for preparing ultrathin, enzymatically active pepsin membranes.
To investigate the potential of these membranes for simultaneous enzymatic conversion and selective removal of digestion products.
To enable large-scale production of stable, active enzyme membranes.

Main Methods:

Facile interfacial polycondensation of pepsin and trimesoyl chloride was employed.
Ultrathin pepsin membranes were synthesized using this polymerization technique.
Membrane properties, including enzymatic activity and water flux, were characterized.

Main Results:

Ultrathin, cross-linked pepsin membranes with high enzymatic activity were successfully prepared.
The membranes facilitated simultaneous enzymatic conversion and selective removal of digestion products.
Large water fluxes through the membranes expedited the transport of large molecules.

Conclusions:

The interfacial polycondensation method provides a facile route to stable, ultrathin pepsin membranes.
These membranes offer a promising platform for efficient enzymatic bioconversion and separation processes.
The developed technique supports the large-scale production of enzymatically active membranes.