An Synthesepulp immobilisierte Enzyme,I.

Synthetic pulp—a polyethylene fibrid which contains poly(vinyl alcohol)—was reacted with 2-(3-aminophenyl)-1,3-dioxolane. The amino derivative was transferred into the reactive diazonium compound. The content of reactive diazonium groups was determined by reaction with tyrosine. The diazonium derivatives of synthetic pulp were used for the immobilization of the hydrolases trypsin, chymotrypsin, papain, aminoacrylase, esterase and urease of the oxidoreductases glucose oxidase, catalase, peroxidase, and glucose-6-phosphate-dehydrogenase, and of the transferase hexokinase. Furthermore soybean trypsin inhibitor was immobilized on synthetic pulp via azo coupling. The protein binding ability of the reactive carriers and the enzymatic properties of the immobilization products were investigated. The thermostability of immobilized trypsin and immobilized urease, as well as the dependence of the immobilized tryptic activity on the temperature were studied. The activities of immobilized trypsin were assayed with low molecular weight substrates as well as with high molecular weight substates. The pH-optima of immobilized chymotrypsin, papain and urease were studied and the influence of buffers on the pH-activity profiles was investigated. Hexokinase and glucose-6-phosphatedehydrogenase were co-immobilized on synthetic pulp as an example for a two enzyme system and the properties of the immobilization products were investigate.