Encapsulation of urease enzyme in xanthan-alginate spheres

Urease-containing xanthan-alginate spheres were prepared by a two-step process which involved the Ca2+ coupling of the polysaccharides, followed by gentle glutaraldehyde cross-linking with amine groups of gelatin present in the initial mixture. This second step caused a slight decrease in the enzymatic activity but increased the stability. The water content and size distribution of the spheres were examined together with the sphere morphology. The effect of polymer ratio and enzyme loading on urease activity was investigated. An increase in xanthan content was found to affect the water uptake of the spheres. Temperature and pH stability of encapsulated urease was found to be higher than the free form. The xanthan-alginate spheres showed 75% of maximum urease activity even after 20 repeated uses under optimal conditions.