| Literature DB >> 30054048 |
Ewa Czechowska1, Katarzyna Ranoszek-Soliwoda1, Emilia Tomaszewska1, Agnieszka Pudlarz2, Grzegorz Celichowski3, Dorota Gralak-Zwolenik4, Janusz Szemraj2, Jaroslaw Grobelny5.
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.Entities:
Keywords: Catalase; Catalase-modified nanoparticles; Enzyme immobilization; Gel electrophoresis
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Year: 2018 PMID: 30054048 DOI: 10.1016/j.colsurfb.2018.07.036
Source DB: PubMed Journal: Colloids Surf B Biointerfaces ISSN: 0927-7765 Impact factor: 5.268