Molecular Cloning, Expression and Enzymatic Characterization of Inosine Monophosphate Dehydrogenase from Bacillus amyloliquefaciens

摘要：

Inosine monophosphate dehydrogenase(IMPDH, Ec1.1.1.205) is the rate-limiting enzyme for de nove guanosine monophosphate synthesis. The IMPDH encoding gene guaB has been clonded and sequenced from Bacillus amyloliquefaciens GR600, a overproduction-guanosine strain. A fragment contained the stuctrural gene guaB encoding IMPDH from GR600 was constructed into expression vector pET-His. The recombinant expression plamid was transformed into Escherichia coil strain BL21(DE3), induced by IPTG and expressed. The recombinat IMPDH was purified by Ni-NTA resins. The result of SDS-PAGE showed that molecular weight of the recombinat IMPDH was 54 kD. Enzyme activity assay showned that the optimum pH value and temperatrure of the recombinat IMPDH were 8.0 and 40 ℃. The results have great significance in genetical modify of producing strain.

作者: Fei Wu Xixian Xie Jianming Shi Qingyang Xu Ning Chen

作者单位: College of Bioengineering Tianjin University of Science and Technology Tianjin, China Key Laboratory of Industrial Microbiology Ministry of Education Tianjin, China

会议类型: 国际会议

会议名称: The 4th International Conference on Bioinformatics and Biomedical Engineering(第四届IEEE生物信息与生物医学工程国际会议 iCBBE 2010)

会议地点: 成都

会议语种:英文

页码: 1-4

在线出版日期: 2010-06-18（万方平台首次上网日期，不代表论文的发表时间）