Expression, Purification And Crystallization Of Xylanase Xyn-E18 And IBDV VP5 Protein

In this paper, a bifunctional xylanase xyn-E18 from Paenibacillus sp. E18 and VP5, which is an nonstructural protein of infectious bursal disease virus (IBDV), were well expressed using E.coli. expression system. Proteins were also purified efficiently after Ni afffinty and Gel filtration chromatography. In addition, crystallizations of xyn-E18 and VP5 protein were tried, but no good crystal was got.Biotechnological applications of xylanases are of increasing importance because of their enormous potential to modify and transform lignocellulosic biomass, used in a wide variety of industrial processes. Xyn-E18, an intracellular xylanase from Paenibacillus sp., catalytes the hydrolysis of both xylan and glucan. In our study, Xyn-E18 was expressed and purified effiently, and crystallization of xyn-E18 was tried using hanging drop method, but no good enough crystal was got.Infectious bursal disease virus (IBDV), a double-stranded RNA (dsRNA) virus from Birnaviridae family, is an economically important avian pathogen. VP5, the nonstructural protein of IBDV, was implicated to play a role in the virus release and cell apoptosis, and it has been expressed insolubly in the previous reports. In our study, extracellular and intracellular regions of vp5 gene were amplified and linked to the vector simultaneously, and two reconstructed gene (vp5-fc/vp5-sc) were expressed and soluble proteins were purified successfully by two steps of chromatography. Crystallization of VP5-SC has been tried, and only some clod-like precipitation was got.