Protein-Repellence PES Membranes Using Bio-grafting of Ortho-aminophenol.

Polymers (Basel)

Department of Materials Science, Institute of Graduate Studies and Research, Alexandria University, Alexandria 21544, Egypt.

Published: August 2016

AI Article Synopsis

  • Surface modification of poly(ethersulfone) (PES) membranes using ortho-aminophenol (2-AP) and laccase enzyme effectively enhances both flux and selectivity by reducing fluid component adsorption.
  • The study evaluates the modified membranes through various techniques such as color change measurement, water flux assessment, and protein repellence tests, correlating results to the grafting yield.
  • Results show that the green modification boosts membrane performance, achieving improvements of 15.4% in flux and 81.27% in protein repellence compared to unmodified membranes.

Article Abstract

Surface modification becomes an effective tool for improvement of both flux and selectivity of membrane by reducing the adsorption of the components of the fluid used onto its surface. A successful green modification of poly(ethersulfone) (PES) membranes using ortho-aminophenol (2-AP) modifier and laccase enzyme biocatalyst under very flexible conditions is presented in this paper. The modified PES membranes were evaluated using many techniques including total color change, pure water flux, and protein repellence that were related to the gravimetric grafting yield. In addition, static water contact angle on laminated PES layers were determined. Blank and modified commercial membranes (surface and cross-section) and laminated PES layers (surface) were imaged by scanning electron microscope (SEM) and scanning probe microscope (SPM) to illustrate the formed modifying poly(2-aminophenol) layer(s). This green modification resulted in an improvement of both membrane flux and protein repellence, up to 15.4% and 81.27%, respectively, relative to the blank membrane.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6432355PMC
http://dx.doi.org/10.3390/polym8080306DOI Listing

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