期刊
PROCESS BIOCHEMISTRY
卷 49, 期 4, 页码 599-603出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2014.01.029
关键词
Secretory expression; Escherichia coli; Recombinant enzymes; Cyclodextrin glycosyltransferase
资金
- National Natural Science Foundation of China [31271813, 31101228]
- Natural Science Foundation of Jiangsu Province [BK2011152]
- Fundamental Research Funds for the Central Universities [JUSRP51304A]
- Fok Ying Tung Education Foundation [131069]
The secretory expression of recombinant enzymes in Escherichia coli has generally been a challenging task. In the present study, we investigated the expression of the extracellular enzyme cyclodextrin glycosyltransferase in E. coli. Our results indicated that when the overexpressed pre-proteins were not translocated across the inner membrane in a timely manner, they aggregated near the inner side of the E. coli inner membrane, resulting in the formation of insoluble inclusion bodies, which eventually blocked the pre-protein translocation channels and subsequently impeded further protein secretion. This mechanism suggests that for the efficient production of extracellular enzymes in E. coli, it is very important to maintain a balance between the rate of pre-protein synthesis and translocation, which can be achieved by altering the cultivation process. Our findings provide novel insight into the secretory expression of extracellular enzymes and may shed light on the further development of new strategies for extracellular protein production in E. coli. (C) 2014 Elsevier Ltd. All rights reserved.
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