Chemistry of Natural Compounds

, Volume 14, Issue 5, pp 540–546 | Cite as

Preparation and properties of enzymes immobilized on supports activated by metal ions

  • V. A. Laurinavichyus
  • Yu. Yu. Kulis


1. Preparations of trypsin, α-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.


Immobilize Enzyme Glucose Oxidase Chymotrypsin Hydroxyquinoline Acryloyl Chloride 


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Copyright information

© Plenum Publishing Corporation 1979

Authors and Affiliations

  • V. A. Laurinavichyus
  • Yu. Yu. Kulis

There are no affiliations available

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