Protein pores packed in polymers make super-efficient filtration membranes

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Protein pores packed in polymers make super-efficient filtration membranes

A multidisciplinary team of engineers and scientists has developed a new class of filtration membranes for a variety of applications, from water purification to small-molecule separations to contaminant-removal processes, that are faster to produce and higher performing than current technology. This could reduce energy consumption, operational costs and production time in industrial separations.

Led by Manish Kumar, associate professor in the Cockrell School of Engineering at The University of Texas at Austin, the research team describes their new high-performance membranes in a recent issue of  Nature Materials .

The team's new filtration membranes demonstrate higher density of pores than that of commercial membranes and can be produced much faster -- in two hours, versus the several-day process currently used. Until now, integrating protein-based membranes into current technology used for industrial separations has been challenging because of the amount of time needed to create these membranes and the low density of proteins in resulting membranes.

This comprehensive and collaborative research effort brought together engineers, physicists, biologists and chemists from UT Austin, Penn State University, University of Kentucky, University of Notre Dame and the company Applied Biomimetic. The work presents the first end-to-end synthesis of a true protein-based separation membrane with pores between half a nanometer and 1.5 nanometers in size. A nanometer is just a few times the size of a water molecule and a hundred thousand times smaller than the width of a human hair.

The membranes created by the team are biomimetic, meaning they mimic systems or elements of nature, and imitate those that naturally occur in cell membranes for transporting water and nutrients. They recently published another paper highlighting the inspiration for their method. High-density packing of these protein channels into polymer sheets forms protein pores within the membrane, similar to those seen in human eye lenses, but within a nonbiological polymer environment.

Three different biomimetic membranes were fabricated by the team and demonstrated a sharp, unique and tunable selectivity with three different pore sizes of membrane protein channels. The methods described can be adapted with the insertion of protein channels of different pore sizes or chemistries into polymer matrices to conduct specifically designed separations.

SOURCE SCIENCE DAILY

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