TY - JOUR
T1 - Separation, Immobilization, and Biocatalytic Utilization of Proteins by a Supramolecular Membrane
AU - Krieg, Elisha
AU - Albeck, Shira
AU - Weissman, Haim
AU - Shimoni, Eyal
AU - Rybtchinski, Boris
N1 - Israel Science Foundation; Minerva Foundation; Gerhardt M.J. Schmidt Minerva Center for Supramolecular Architectures; Helen and Martin Kimmel Center for Molecular Design; Yeda Sela Center for Basic ResearchThis work was supported by grants from the Israel Science Foundation, the Minerva Foundation, the Gerhardt M.J. Schmidt Minerva Center for Supramolecular Architectures, the Helen and Martin Kimmel Center for Molecular Design, and the Yeda Sela Center for Basic Research. E. K. acknowledges the Minerva PhD fellowship. B. R. holds the Abraham and Jennie Fialkow Career Development Chair. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
PY - 2013/5/10
Y1 - 2013/5/10
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84877597108&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0063188
DO - 10.1371/journal.pone.0063188
M3 - مقالة
C2 - 23675461
SN - 1932-6203
VL - 8
JO - PLoS ONE
JF - PLoS ONE
IS - 5
M1 - e63188
ER -