文献类型：期刊文献

中文题名：表达双功能谷胱甘肽合成酶的重组巴斯德毕赤酵母的构建与鉴定

英文题名：Construction and identification of recombinant Pichia pastoris expressing novel bifunctional glutathione synthetase

作者：杨建花[1];李娓[1];王德正[1];李志敏[1];叶勤[1]

机构：[1]华东理工大学生物反应器工程国家重点实验室,上海200237

年份：2013

卷号：43

期号：5

起止页码：63

中文期刊名：工业微生物

外文期刊名：Industrial Microbiology

收录：CSCD:【CSCD_E2013_2014】；

基金：生物反应器工程国家重点实验室面上项目;上海市科委产学研医合作重点项目资助(13DZ1930202)

语种：中文

中文关键词：谷胱甘肽;双功能谷胱甘肽合成酶;毕赤酵母

外文关键词：glutathione; bifunctional glutathione synthetase; Pichia pastoris

摘要：通过PCR获得来自于嗜热链球菌中的双功能谷胱甘肽合成酶基因gshF,插入表达载体pGAPZA,转化巴斯德毕赤酵母GS115,成功构建了表达外源双功能谷胱甘肽合成酶基因的重组毕赤酵母。重组茵经摇瓶发酵,并在培养过程中添加前体半胱氨酸,96 h后生成的GSH是宿主茵的2.23倍。
The gshF gene was cloned from Streptococcus therrnophilus SlIM B218 by PCR, and was inserted in the expression vector pGAPZA. The recombinant plasmid was transformed into Pichia pastoris GS115 to construct a recombinant P. pastoris strain expressing the gene coding for the novel bifunctional glutathione synthetase GshF. The capability to synthe- size glutathione by this strain was examined in shake-flask cultivation in the presence of cysteine. The glutathione content in the recombinant cells was 2.23 times than that in the host cells. The genetic engineering GS115 in this work had high potential in GSH production by fermentation.