Immobilized Enzymes Catalysis Reviews. 1978
- 1 January 1980
- journal article
- research article
- Published by Taylor & Francis in Catalysis Reviews
- Vol. 22 (1) , 29-73
- https://doi.org/10.1080/03602458008066529
Abstract
Enzymes are protein catalysts found in all living cells. For more than a century chemists and biochemists have been studying the structure and function of these remarkable molecules, It is now known that the majority of enzymes are globular in structure with molecular weights in the range of 10, 000 to 600, 000 (Fig. 1). The active center, which generally represents a relatively small portion of the surface area of the molecule, is composed of a binding site and a catalytic site. In addition to amino acid side chains such as imidazole and thiol groups, the catalytic site often contains metal ions and non-protein “coenzymes”.Keywords
This publication has 98 references indexed in Scilit:
- Kinetics of a hollow fiber dehydrogenase reactorBiotechnology & Bioengineering, 1975
- Immobilization of enzymes on aldehydic matrices by reductive alkylationBiochemical and Biophysical Research Communications, 1975
- Preparation of immobilized enzymes from acrylic monomers under γ‐ray irradiationBiotechnology & Bioengineering, 1975
- The preparation and characterisation of a water‐soluble coenzymically active dextran‐NAD+FEBS Letters, 1974
- Protein binding by agarose carrying hydrophobic groups in conjunction with chargesBiochemical and Biophysical Research Communications, 1973
- The preparation of some immobilised dehydrogenases and their use in automated analysisFEBS Letters, 1972
- Glutaraldehyde: Nature of the reagentJournal of Molecular Biology, 1972
- Preparation and properties of urease chemically attached to nylon tubeFEBS Letters, 1970
- Glutaraldehyde as a protein cross-linking reagentJournal of Molecular Biology, 1968
- A Water-insoluble Trypsin Derivative and its Use as a Trypsin ColumnNature, 1960