| Abstract: | Summary 1. Preparations of trypsin,  -chymotrypsin, and glucose oxidase immobilized on synthetic and polysaccharide supports charged with transition-metal ions contain 3–64 mg of protein per 1 g of support.2. The activity of immobilized enzymes amounts to 100–10,000 U/g. The activity yield is 2.2–90X%.3. The pH dependence of the enzymes is shifted in the alkaline direction by 0.26–1.19 units. The Michaelis constants and inhibitor constants have decreased by factors of 1.5–21.4. The mechanism of the fixation of enzymes is determined by the formation of coordination bonds and by inclusion in inorganic gels. The properties of the enzymes are due to the surface charge of the activated supports.Institute of Biochemistry, Academy of Sciences of the Lithuanian SSR, Vilnius. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 629–637, September–October, 1978. |
