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The sensitivity of immobilized enzymes to the magnetic core of various carriers

Autoři: Ježová Jana | Korecká Lucie | Hradcová Olga | Bílková Zuzana

Rok: 2004

Druh publikace: ostatní - přednáška nebo poster

Název zdroje: 9th International Symposium on BIOCHROMATOGRAPHY ?From nanoseparations to macropurificationsˇ§

Název nakladatele: Society for biochromatography and nanoseparations

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Jazyk	Název	Abstrakt	Klíčová slova
cze	Citlivost imobilizovaných enzymů k magnetickému jádru různých nosičů	Citlivost imobilizovaných enzymů k magnetickému jádru různých nosičů	IMER; magnetic particles
eng	The sensitivity of immobilized enzymes to the magnetic core of various carriers	Immobilized enzyme technology has grown rapidly during last decades, the enzyme reactors have utilized in many application areas of biotechnology where specific modification of target molecules or/and catalysis of chemical reactions is needed. Enzymes can be physically adsorbed or covalently attached to a support or entrapped within a matrix or membrane1. Enzyme immobilization provides many advantages over use of enzymes in soluble form: controlled product formation, enhanced enzyme activity, simplified and efficient processing and enzyme reusability. The storage properties and the pH stability of enzymes are often improved by immobilization2. In order to utilize advantages of magnetic supports as simplicity of separation from the reaction mixture and considerate handling with a sample, enzymes can be immobilized on various supports with magnetic core. However, some enzymes lose their activity if they are immobilized on magnetic support. In some cases the activity of enzyme rapidly decreases because of its sensitivity to the magnetic core. In order to compare the sensitivity of selected enzymes to the magnetic core of supports (alginate coated ferrite microparticles, polyNIPAM Ademtech nanoparticles, magnetic bead macroporous cellulose) we have immobilized four enzymes: chymotrypsin, neuraminidase, ?Ň-D-galactosidase and trypsin. We have been observing the storage and operational stability of all enzyme reactors. As control we have utilized non-magnetic versions of these carriers. The proteolytic activity of immobilized trypsin measured immediately after immobilization and during one month was very high and stable in contrast to zero activity of chymotrypsin both immobilized to the alginate coated ferrite microparticles. The relatively high neuraminidase activity after immobilization has decreased rapidly to zero activity after one week. Meanwhile the glycosidic activity of immobilized ?Ň-D-galactosidase has been gradually decreasing during two weeks. The sensit	IMER; magnetic particles

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