Comparison of the antioxidant activity of catalase immobilized on gold nanoparticles via specific and non-specific adsorption

Colloids Surf B Biointerfaces. 2018 Nov 1:171:707-714. doi: 10.1016/j.colsurfb.2018.07.036. Epub 2018 Jul 20.

Abstract

In this study, we present a comparison of the antioxidant activity of catalase immobilized on gold nanoparticles (AuNPs) by two methods: i) directly on the surface of AuNPs (non-specific immobilization), and ii) via chemical bonding using a linker (specific immobilization). Quantification of the enzyme amount adsorbed on the nanoparticle surface was determined by native-polyacrylamide gel electrophoresis (native-PAGE). Colloidal stability of AuNPs before and after the enzyme immobilization was monitored with dynamic light scattering (DLS) and UV-vis spectroscopy. The size of the metallic core was determined by scanning-transmission electron microscopy (STEM). The enzymatic activity of catalase immobilized on AuNPs was investigated by antioxidant tests and compared with free (non-immobilized) catalase. It was found that the activity of catalase immobilized on AuNPs is affected by the immobilization method. Moreover, it was found that the non-specific immobilization decreased the antioxidant activity while the specific immobilization of catalase allowed the catalase activity to remain at the same level as that of free catalase.

Keywords: Catalase; Catalase-modified nanoparticles; Enzyme immobilization; Gel electrophoresis.

Publication types

  • Comparative Study

MeSH terms

  • Adsorption
  • Antioxidants / chemistry
  • Antioxidants / metabolism*
  • Catalase / chemistry
  • Catalase / metabolism*
  • Enzymes, Immobilized / chemistry
  • Enzymes, Immobilized / metabolism*
  • Gold / chemistry
  • Gold / metabolism*
  • Metal Nanoparticles / chemistry*
  • Models, Molecular
  • Molecular Structure
  • Particle Size
  • Surface Properties

Substances

  • Antioxidants
  • Enzymes, Immobilized
  • Gold
  • Catalase