中文摘要：

[目的]提高蓝藻抗病毒蛋白-N（CVN）的异源表达量,获得大量高纯度可溶性蛋白。[方法]采用RT-PCR从酱油发酵酱醪宏基因组中克隆获得CVN基因cvn-SF,构建了重组表达载体p ET32a-cvn-SF,转化E.coli BL21菌株,获得工程菌株,优化表达条件,通过Ni-NTA凝胶亲和层析对CVN-SF蛋白进行纯化。[结果]工程菌株在温度30℃、添加1 mmol/L的IPTG诱导剂、培养时间12 h的条件下获得最高表达量的可溶性蛋白。Ni-NTA凝胶亲和层析纯化得到了230.8 mg/L的CVN蛋白,占提取总蛋白含量的33.37%。[结论]所得CVN蛋白高于目前报道的CVN在大肠杆菌的最高表达量140 mg/L^（[11]）。

英文摘要：

[Objective] A recombinant was constructed to obtain abundant water-soluble CVN protein by the heterologous expression. [Methods] CVN gene was cloned from fermented soybean sauce and constructed into the p ET32 a expression vector.The recombinant protein was expressed in the cytoplasm of E. coli BL21 in a soluble form. Ni-NTA affinity chromatography was used to purify it. [Results]SDS-PAGE assay showed that recombinant CVN was expressed and purified successfully. Meanwhile,the optimal induction conditions were selected. [Conclusion] 230. 8 mg / L purified CVN protein was obtained,which was more than the maximum that had been reported.