Surface modification of polymeric membranes for low protein binding

Akon Higuchi, Miho Tamai, Yoh Ichi Tagawa, Yung Chang, Qing Dong Ling

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Surface modification of microfiltration and ultrafiltration membranes has been widely used to improve the protein adsorption resistance and permeation properties of hydrophobic membranes. Several surface modification methods for converting conventional membranes into low-protein-binding membranes are reviewed. They are categorized as either physical modification or chemical modification of the membrane surface. Physical modification of the membrane surface can be achieved by coating it with hydrophilic polymers, hydrophilic-hydrophobic copolymers, surfactants or proteins. Another method of physical modification is plasma treatment with gases. A hydrophilic membrane surface can be also generated during phase-inverted micro-separation during membrane formation, by blending hydrophilic or hydrophilichydrophobic polymers with a hydrophobic base membrane polymer. The most widely used method of chemical modification is surface grafting of a hydrophilic polymer by UV polymerization because it is the easiest method; the membranes are dipped into monomers with and without photo-initiators, then irradiated with UV. Plasma-induced polymerization of hydrophilic monomers on the surface is another popular method, and surface chemical reactions have also been developed by several researchers. Several important examples of physical and chemical modifications of membrane surfaces for low-protein-binding are summarized in this article.

Original languageEnglish
Pages (from-to)103-120
Number of pages18
JournalMembrane Water Treatment
Volume1
Issue number2
DOIs
StatePublished - Apr 2010

Keywords

  • Biofouling
  • Fouling
  • Low-protein-binding.
  • Microfiltration
  • Surface modification
  • Ultrafiltration

Fingerprint

Dive into the research topics of 'Surface modification of polymeric membranes for low protein binding'. Together they form a unique fingerprint.

Cite this