Separation, Immobilization, and Biocatalytic Utilization of Proteins by a Supramolecular Membrane

13Citations
Citations of this article
20Readers
Mendeley users who have this article in their library.

Abstract

Membrane separation of biomolecules and their application in biocatalysis is becoming increasingly important for biotechnology, demanding the development of new biocompatible materials with novel properties. In the present study, an entirely noncovalent water-based material is used as a membrane for size-selective separation, immobilization, and biocatalytic utilization of proteins. The membrane shows stable performance under physiological conditions, allowing filtration of protein mixtures with a 150 kDa molecular weight cutoff (∼8 nm hydrodynamic diameter cutoff). Due to the biocompatibility of the membrane, filtered proteins stay functionally active and retained proteins can be partially recovered. Upon filtration, large enzymes become immobilized within the membrane. They exhibit stable activity when subjected to a constant flux of substrates for prolonged periods of time, which can be used to carry out heterogeneous biocatalysis. The noncovalent membrane material can be easily disassembled, purified, reassembled, and reused, showing reproducible performance after recycling. The robustness, recyclability, versatility, and biocompatibility of the supramolecular membrane may open new avenues for manipulating biological systems.

Cite

CITATION STYLE

APA

Krieg, E., Albeck, S., Weissman, H., Shimoni, E., & Rybtchinski, B. (2013). Separation, Immobilization, and Biocatalytic Utilization of Proteins by a Supramolecular Membrane. PLoS ONE, 8(5). https://doi.org/10.1371/journal.pone.0063188

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free