Immobilization of enzymes on 2-hydroxyethyl methacrylate and glycidyl methacrylate copolymer brushes

Chem Asian J. 2014 Aug;9(8):2132-9. doi: 10.1002/asia.201402150. Epub 2014 Jun 24.

Abstract

The immobilization of enzymes is of paramount importance to maintain their activity and stability. In this study, surface-initiated atom-transfer radical polymerization was applied to prepare poly(2-hydroxyethyl methacrylate)-block-poly(2-hydroxyethyl methacrylate-co-glycidyl methacrylate) brushes on glass slides. The polymerization kinetics was followed by using a quartz crystal microbalance with dissipation monitoring and ellipsometry in terms of mass and thickness growth, respectively. The surface chemical compositions of the obtained polymer brushes were characterized by X-ray photoelectron spectroscopy. Their mass, thickness, and enzyme-immobilization ability could be easily tuned by the initiator reaction time, monomer ratio, and polymerization time. The antibacterial activity and stability of the immobilized lysozymes were studied by fluorescent staining and bacteria lysis assay, which revealed that the lysozymes on the copolymer brushes had good stability during storage at 4 °C for up to 30 days.

Keywords: copolymerization; enzymes; immobilization; polymers; surface chemistry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteria
  • Enzymes, Immobilized / chemistry*
  • Epoxy Compounds / chemistry*
  • Methacrylates / chemistry*
  • Muramidase / chemistry
  • Photoelectron Spectroscopy
  • Polymers / chemistry*

Substances

  • Enzymes, Immobilized
  • Epoxy Compounds
  • Methacrylates
  • Polymers
  • hydroxyethyl methacrylate
  • Muramidase
  • glycidyl methacrylate