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By Sameh Magdeldin

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1998). Fig. 4. Recombinant protein preparation It should be once more emphasized that only one of the simplest strategies for recombinant protein production was described and for more precise description of cloning methods, gene manipulations and expression system advantages the reader is recommended to search in mentioned works. 3 Affinity tags used for protein immobilization As stated earlier, following paragraphs will discuss the most interesting affinity tags, which were used for enzyme immobilization.

Second part of this chapter will explain the reasons for recombinant proteins preparation and the advantage of proteins modifications by techniques of molecular biology. A simple strategy for recombinant protein preparation in the simplest expression system of E. coli will be described for a better comprehensibility. Different methods of exploitation of affinity interactions for the protein immobilization will be referred in the last part of the chapter. The importance of achieved results for the biotechnological practice will be summarized.

Immobilization methods exploiting binding to a carrier. 2 Enzyme molecules cross-linking In these methods bi- or multifunctional compounds are used for cross-linking of desired enzyme molecules (figure 2). Lysines amino groups are usually involved in covalent bonds formation; however, other amino acids functional groups may be used, too. g. , 2005; Sheldon, 2007; Tischer & Wedekind, 1999). Fig. 2. 3 Entrapment The basis of this method is the inclusion of the biocatalyst within a polymeric network of different types (figure 3).

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