Silk consists of two main proteins called fibroin and sericin. While fibroin is used in textile production and various biomaterial applications, sericin is considered as waste material in the textile industry. Sericin is a multi-component protein with an indefinite structure and it has been shown to be biocompatible and has biological activity. Because of the positive effects on keratinocytes and fibroblasts have led to the development of sericin-based biomaterials for the repair of skin tissue. Sericin from silkworm cocoons can be obtained by chemical treatment, enzymatic treatment and boiling in water. Although sericin can be separated from fibroin by chemical, enzymatic and boiling in water treatment methods, all these treatment methods are not enough to obtain recovery of high-quality sericin. Moreover, in these treatment methods, the exposure of sericin protein to high temperature causes even sericin protein obtained by the same method to indicate different characteristics. The fact that the obtained sericin demonstrate such major changes in the structure according to treatment methods bring inconsistencies in the quality of sericin produced as a biomaterial. The aim of the study is to produce native sequence of sericin that forms a tetramer contain each containing 38 amino acids with recombinant production in E.coli and to characterize structural properties Thus, obtaining sericin protein from the bacteria with recombinant methods will solve these problems in question The results indicate that for the first time, the conformational properties of recombinant sericin were obtained similar to the native sericin structure.