Preparation of Membranous Immobilized Invertase and It’s Characteristics

Abstract
Invertase was immobilized by radiocopolymerization of some synthetic monomers which were mixed in various combinations. Irradiation was conducted aerobically while the mixture of monomers and enzyme was frozen. Retained activity was 51~76%. Immobilized invertase shifted its optimum pH by about 0.7 to the acidic site. The optimum reaction temperature of enzyme became a little higher (Ca 5°C) by immobilization. Heat stability was improved by immobilization. Release of fixed enzyme was found to be considerably low (1.2~4.1%) and release of several immobilized proteins decreased as the molecular weight increased.

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