Abstract

The catalase (E.C. 1.11.1.6) enzyme was covalently immobilized on textile carrier fabrics made of poly(ethylene terephthalate) or polyamide 6.6 by a new photochemical process in the presence of cross-linking agents. The enzyme and the bifunctional organic compound (diallylphthalate or cyclohexane-1,4-dimethanoldivinylether) were emulated in water using a non-ionic surfactant. After wetting, the textile carrier materials were irradiated with a monochromatic excimer UV lamp (222 nm) in an inert atmosphere. Depending on the support and the cross-linking agent used 20 – 30 mg enzyme per gram carrier could be fixed durably, which can be quantitatively analyzed by atomic absorption spectroscopy due to the iron content of the catalase. The efficiency of the immobilization products was investigated by measuring the enzymatic decomposition of hydrogen peroxide compared to the free enzyme. The relative activity of the catalase after the immobilization reached 10–20 % of the free, non-fixed catalase. Even after 20 applications, the immobilized enzyme showed a distinct activity and the integral activity trough the period of all applications was higher by a factor of around 3.5 than the activity of the free catalase, which could be used only once in technical processes. Summing up the results, fabrics of a high protein load and a distinct activity can be produced with low preparative and economic expense by irradiating the materials by means of excimer UV lamps in the presence of cross-linking agents.

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