Oriented immobilization of galactose oxidase to bead and magnetic bead cellulose and poly(HEMA-co-EDMA) and magnetic poly(HEMA-co-EDMA) microspheres
Language English Country Netherlands Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12013233
DOI
10.1016/s0378-4347(01)00439-x
PII: S037843470100439X
Knihovny.cz E-resources
- MeSH
- Cellulose chemistry MeSH
- Enzymes, Immobilized chemistry MeSH
- Galactose Oxidase chemistry MeSH
- Immunoglobulin G chemistry MeSH
- Periodic Acid chemistry MeSH
- Magnetics MeSH
- Methacrylates chemistry MeSH
- Microspheres MeSH
- Nuclear Magnetic Resonance, Biomolecular MeSH
- Polyhydroxyethyl Methacrylate chemistry MeSH
- Swine MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Cellulose MeSH
- Enzymes, Immobilized MeSH
- ethylene dimethacrylate MeSH Browser
- Galactose Oxidase MeSH
- Immunoglobulin G MeSH
- Periodic Acid MeSH
- metaperiodate MeSH Browser
- Methacrylates MeSH
- Polyhydroxyethyl Methacrylate MeSH
In order to obtain an active and stable oxidation reactor for daily use in biochemical laboratory we decided to immobilize galactose oxidase orientedly through a carbohydrate chain to the magnetic carriers. We used hydrazide derivatives of non-magnetic and magnetic bead cellulose and of magnetic and non-magnetic poly(HEMA-co-EDMA) microspheres. Activation of the enzyme molecules was done by sodium periodate in the presence of supplements (fucose, CuSO4, catalase). Orientedly immobilized galactose oxidase presents high storage stability and lower susceptibility to inappropriate microenvironmental conditions. Reactor reactivated by three pulses of D-galactose retained practically 100% of its native activity after 6 months. The positive properties of both magnetic carriers were entirely confirmed.
References provided by Crossref.org
