The use of alkaline protease as commercial catalysts has increased significantly in recent years. Often main industrial and commercial uses, like the food fabric and medical diagnostics industries depend heavily on the protease enzyme. The free movement of enzymes is constrained in the cell immobilization technique and a continuous fermentation method can be used. The procedure was usually used with different carriers, such as chitosan, agar and alginate, to create alkaline proteases. In conjunction to the encapsulation of an enzyme using an Encapsulator instrument, we attempted to use this technique to examine the implementation of individual matrices to immobilize the protease enzyme. This enzyme was previously recovered from Bacillus Pseudofirmus Mn6 EU315248. Some physical characteristics of the immobilized enzyme such as activity temperature, pH effect and operational stability were assessed. Results revealed that the maximum pH stability attained throughout the chitosan matrix-entrapped enzyme, when incubated at pH of 10.5 for 15min. is nearly 200%.  The protease enzyme immobilized in chitosan, displayed excellent stability when incubated at 50^oC for 1h with a local detergent. The enzyme retained its maximal activity even after 1h of incubation with the majority of the tested detergents. Washing performance of the immobilized alkaline protease was also applied on two types of dirty cloth spots, i.e. blood and chocolate spots. Results confirmed that the immobilized protease enzyme must be used as one of the ingredients in the detergents industry.