生物技术通报 ›› 2016, Vol. 32 ›› Issue (11): 255-260.doi: 10.13560/j.cnki.biotech.bull.1985.2016.11.033

• 研究报告 • 上一篇    下一篇

CydDC蛋白的表达及对谷胱甘肽运输的影响

全聪, 张静, 吴辉, 李志敏, 叶勤   

  1. 华东理工大学 生物反应器工程国家重点实验室,上海 200237
  • 收稿日期:2016-03-23 出版日期:2016-11-25 发布日期:2016-11-11
  • 作者简介:全聪,男,硕士,研究方向:发酵工程;E-mail:masterjackiequan@163.com
  • 基金资助:
    上海市产学研医合作项目

Expression of CydDC in Escherichia coli and the Effect of It on Glutathione Transportation

QUAN Cong, ZHANG Jing, WU Hui, LI Zhi-min, YE Qin   

  1. State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology,Shanghai 200237
  • Received:2016-03-23 Published:2016-11-25 Online:2016-11-11

摘要: 在重组大肠杆菌中共表达了谷胱甘肽运输蛋白CydDC与双功能合成酶GshF,通过增强对谷胱甘肽的运输作用,提高谷胱甘肽产量。实验结果表明,目的蛋白CydDC及GshF均成功表达;重组菌MG1655(pTrc99a-as/pBAD33-cydDC)总谷胱甘肽产量为0.22 mmol/L,胞外谷胱甘肽含量显著增加,达到81.9%,分别是对照菌MG1655(pTrc99a-as/pBAD33)的1.11倍和1.29倍。

关键词: 谷胱甘肽, 运输蛋白, 共表达, 重组大肠杆菌

Abstract: This study is to co-express the CydDC and GshF in the recombinant Escherichia coli,and to increases the glutathione production by enhancing glutathione transportation. As the results from the experiments,the target protein CydDC and GshF were successfully expressed,the glutathione production of MG1655(pTrc99a-as/pBAD33-cydDC)reached 0.22 mmol/L,and the content of glutathione in supernatant significantly increased and reached 81.9%,which was 1.11-fold and 1.29-fold of control strain MG1655(pTrc99a-as/pBAD33),respectively.

Key words: glutathione, transporter, co-expression, recombinant Escherichia coli