Immobilized enzyme
An immobilized enzyme is an enzyme attached to an inert, insoluble material—such as calcium alginate (produced by reacting a mixture of sodium alginate solution and enzyme solution with calcium chloride). This can provide increased resistance to changes in conditions such as pH or temperature. It also lets enzymes be held in place throughout the reaction, following which they are easily separated from the products and may be used again - a far more efficient process and so is widely used in industry for enzyme catalysed reactions. An alternative to enzyme immobilization is whole cell immobilization. Commercial use. Immobilized  enzymes are very important for commercial uses as they possess many benefits to the expenses and processes of the reaction of which include: In the past, biological washing powders and detergents contained many proteases and lipases that broke down dirt. However, when the cleaning products contacted human skin, they created allergic reactions. This is why immobilization of enzymes are important, not just economically. Immobilization of an enzyme. There are various ways by which one can immobilize an enzyme: Random versus Site-directed Enzyme Immobilization. Numerous enzymes of biotechnological importance have been immobilized on various supports (inorganic, organic, composite and nanomaterials ) via random multipoint attachment. However, immobilization via random chemical modification results in a heterogeneous protein population where more than one side chains (amino, carboxyl, thiol etc) present in proteins are linked with the support with potential reduction in activity due to restriction of substrate access to the active site. In contrast, in site-directed enzyme immobilization, the support can be linked to a single specific amino acid (generally N- or C-termini) in a protein molecule away from the active-site. This way maximal enzyme activity is retained due to the free access of the substrate to the active-site . These strategies are mainly chemical but may additionally require genetic and enzymatic methods to generate functional groups (that are absent in protein) on the support and enzyme. The choice of SDCM method depends on many factors, such as the type of enzyme (less stable psychrophilic, or more stable thermophilic homologue), pH stability of enzyme, the availability of N- or C-termini to the reagent, non-interference of the enzyme terminus with the enzyme activity, type of catalytic amino acid residue, the availability, price and the ease of preparation of reagents. For example, the generation of complementary clickable functionalities (alkyne and  azide) on the support and enzyme is one of the most convenient way for immobilizing enzymes via site-directed chemical modification. Immobilization of a Substrate for Enzymatic Reactions. Another widely used application of the immobilization approach together with enzymes has been the enzymatic reactions on immobilized substrates. This approach facilitates the analysis of enzyme activities and mimics the performance of enzymes on e.g. cell walls.