Immobilised enzymes have an enormous potential as catalysts in chemical processes in a wide range of industries and medicine. They offer a distinct advantage over classical catalyst due to their specificity, high catalytic efficiency at low temperatures and, being biodegradable, present fewer disposable problems (Bullock, 1995). The use of immobilised enzymes lowers production costs as the immobilised enzymes can readily be separated from reaction mixtures and hence can be used repeatedly or continuously. Many different methods have been employed for enzyme immobilisations including adsorption onto insoluble materials, entrapment in polymeric gels, encapsulation, cross-linking with bifunctional or multifunctional reagents and linking to an insoluble carrier (Cao, 2005). The gel entrapment method has the advantage that it preserves a high level of enzyme activity since enzyme molecules are physically retained and shielded by the matrix and not chemically bound to it. The immobilisation of enzymes in their active state may increase their potential application for industrial purposes (Milovanović, Božić, & Vujčić, 2007). The main disadvantage of the entrapment immobilised enzymes is their leak out. Diffusion effects are drawback in gel entrapment protocols as the substrate must diffuse through the gel to reach enzyme molecules buried inside the matrix.