ABSTRACT
An immobilization technique was attempted for the first time in 1916 by Nelson and Griffin with the enzyme invertase being immobilized onto an activated charcoal support, but it wasn't until the 1960s before research into enzyme immobilization gained traction. Immobilization of the biocatalyst, particularly enzymes, is typically carried out by one of three different methods, i.e., cross-linked matrices, encapsulation and microencapsulation. Microencapsulation is a versatile immobilization procedure because it allows simultaneous entrapment of different enzymes, cofactors because they are linked to hydrophilic polymers. The addition of a cross-linking agent can be made to an enzyme already adsorbed onto the support, or onto the free enzyme followed by adsorption onto the support. As the immobilization is an artificial technique, effects on the catalytic activity are observed, i.e., steric, conformational, diffusion, mass transport and related to the microenvironment. Since the sixties of the last century when the immobilization technique was invented a lot of applications were observed in industry, chemical, biomedical analysis.
