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Interaction of Enzyme with Polymer Matrix in Immobilized Enzymes

✍ Scribed by Minoru Kumakura; Isao Kaetsu

Publisher
John Wiley and Sons
Year
1983
Tongue
German
Weight
275 KB
Volume
66
Category
Article
ISSN
0018-019X

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✦ Synopsis

Abstract

Thermolysin was immobilized by radiation polymerization of hydroxyalkyl acrylate and tetradecaethylene glycol dimethacrylate monomers at low temperatures in the presence of the enzyme, and the degree of interaction of the enzyme with the polymer matrix was studied by measuring the thermal stability of the immobilized enzyme. The thermal stability was affected by the molecular structure of the monomer; the thermal stability of the immobilized enzyme from hydrophilic monofunctional monomers in the wet state was higher than that from hydrophobic bifunctional monomers. The thermal stability in polymers formed from hydroxy‐alkyl acrylates decreased with an increase in the number of methylene units in the monomer, owing to a change of the state of the enzyme trapped in the porous polymer matrix. The enzyme molecule trapped in a hydrophilic porous polymer matrix appeared to be stabilized by interaction with the polymer chains.

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