Abstract
Adsorption, covalent bonding, and occlusion into the structure of a gel can be used to attach enzymes to insoluble carriers in order to obtain heterogeneous enzymic catalysts. The kinetic characteristics of the enzymes are affected by immobilisation, but these changes – quite often more apparent than real – are due to changes not in the properties of the enzyme molecules themselves but in their microenvironment. Immobilised enzymes possess enhanced stability, and can be employed in technical processes, biochemical analyses, and medicine.
A list of 506 references is included.