Efficient soluble expression of disulfide bonded proteins in the cytoplasm of Escherichia coli in fed-batch fermentations on chemically defined minimal media
作者: Anna GąciarzNarendar Kumar KhatriM. Lourdes Velez-SuberbieMirva J. SaaranenYuko UchidaEli Keshavarz-MooreLloyd W. Ruddock
作者单位: 1University of Oulu
2University College London
刊名: Microbial Cell Factories, 2017, Vol.16 (1)
来源数据库: Springer Nature Journal
DOI: 10.1186/s12934-017-0721-x
关键词: Disulfide bondsCytoplasmEscherichia coliFermentationFed-batchInterleukin 6Growth hormoneScFvAvidin
原始语种摘要: The production of recombinant proteins containing disulfide bonds in Escherichia coli is challenging. In most cases the protein of interest needs to be either targeted to the oxidizing periplasm or expressed in the cytoplasm in the form of inclusion bodies, then solubilized and re-folded in vitro. Both of these approaches have limitations. Previously we showed that soluble expression of disulfide bonded proteins in the cytoplasm of E. coli is possible at shake flask scale with a system, known as CyDisCo, which is based on co-expression of a protein of interest along with a sulfhydryl oxidase and a disulfide bond isomerase. With CyDisCo it is possible to produce disulfide bonded proteins in the presence of intact reducing pathways in the cytoplasm.
全文获取路径: Springer Nature  (合作)
影响因子:3.306 (2012)

  • disulfide 二硫化物
  • expression 表示
  • Escherichia 埃希氏菌属
  • proteins 蛋白质
  • cytoplasm 细胞质
  • bonded 保税
  • batch 一批
  • periplasm 周质
  • isomerase 异构酶
  • soluble 可溶的