جستجوی مقالات مرتبط با کلیدواژه "تراریختگی" در نشریات گروه "زیست شناسی"

Today, using genetic engineering, recombinant proteins can be produced in large volumes, desirable quality and low cost to meet the demands of different industries. The recombinant proteins can be expressed in various expression methods such as cell-free expression systems or prokaryotic or eukaryotic cells. Considering the advantages of using prokaryotic cells, one of the commonly used systems for the production of recombinant proteins is the cultivation of Escherichia coli (E. coli). The aim of the present study was to evaluate the expression of recombinant protein in E. coli and provide a suitable methods for achieving high cell density and maximal expression capability. Hence, by studying about 63 published articles in the field of genetic engineering, various expression systems were introduced for recombinant proteins production. In spite of many advantages and vast applications for this method of recombinant protein production, its use may include problems such as false folding, production of aggregated proteins and the absence of expression of soluble and active ones. Several approaches have been developed to increase the efficiency and solubility; change in the rate of synthesis of proteins, use of binding proteins, mutations in the target protein, simultaneous expression of molecular chaperones and optimization of culture conditions, are among different methods which is evaluated in this study. Virtual cloning has come into the context of developing more advanced software tools and databases and has been able to eliminate the limitations of recombinant expression of proteins in hosts with a different expression system.