Catalysts (Apr 2020)

Polymer Membrane with Glycosylated Surface by a Chemo-Enzymatic Strategy for Protein Affinity Adsorption

  • Yan Fang,
  • Ting He,
  • Hao Gao,
  • Lingling Fan,
  • Jingyuan Liu,
  • Binrui Li,
  • Haowei Zhang,
  • Huiyu Bai

DOI
https://doi.org/10.3390/catal10040415
Journal volume & issue
Vol. 10, no. 4
p. 415

Abstract

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Membranes with glycosylated surfaces are naturally biomimetic and not only have excellent surface hydrophilicity and biocompatibility, but have a specific recognition to target biomacromolecules due to the unique chemo-biological properties of their surface carbohydrates; however, they cannot be easily chemically produced on large scales due to the complex preparation process. This manuscript describes the fabrication of a polypropylene membrane with a glycosylated surface by a chemo-enzymatic strategy. First, hydroxyl (OH) groups were introduced onto the surface of microporous polypropylene membrane (MPPM) by UV-induced grafting polymerization of oligo(ethylene glycol) methacrylate (OEGMA). Then, glycosylation of the OH groups with galactose moieties was achieved via an enzymatic transglycosylation by β-galactosidase (Gal) recombinanted from E. coli. The fabricated glycosylated membrane showed surprisingly specific affinity adsorption to lectin ricinus communis agglutinin (RCA120). The chemo-enzymatic route is easy and green, and it would be expected to have wide applications for large-scale preparation of polymer membranes with glycosylated surfaces.

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