Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration

2005 ◽  
Vol 39 (1) ◽  
pp. 54-60 ◽  
Author(s):  
Pernilla Turner ◽  
Olle Holst ◽  
Eva Nordberg Karlsson
2020 ◽  
Vol 30 (1) ◽  
pp. 109-117
Author(s):  
A-Hyeon Kim ◽  
Soohyun Lee ◽  
Suwon Jeon ◽  
Goon-Tae Kim ◽  
Eun Jig Lee ◽  
...  

2017 ◽  
Vol 47 (6) ◽  
pp. 619-626 ◽  
Author(s):  
Qinghua Tian# ◽  
Ping Zhang# ◽  
Zhan Gao ◽  
Hengli Li ◽  
Zhengli Bai ◽  
...  

PLoS ONE ◽  
2013 ◽  
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pp. e56363 ◽  
Author(s):  
Min-Feng Hsu ◽  
Tsung-Fu Yu ◽  
Chia-Cheng Chou ◽  
Hsu-Yuan Fu ◽  
Chii-Shen Yang ◽  
...  

2014 ◽  
Vol 14 (1) ◽  
pp. 5 ◽  
Author(s):  
Sujuan Yuan ◽  
Xin Wang ◽  
Jian Xu ◽  
Zheng Yan ◽  
Nan Wang

2019 ◽  
Vol 16 (3) ◽  
pp. 162
Author(s):  
Le Duong Vuong ◽  
Le Thi Tuong Vy ◽  
Phan Thi Phuong Trang ◽  
Nguyen Duc Hoang

The Human rhinovirus 3C protease (HRV3C) is one of the most effective enzymes for removing fusion tag in purification process. This protease is often produced as fusion form GST-HRV3C but there is no study about the fusion form: GST-HRV3C-His. In this study, researchers conducted the purification GST-HRV3C-His expressed in E. coli, checked the activity and investigated its application. GST-HRV3C-His could be purified using His-tag column with 86.6% purity and GST column with 96.87%. The specific activity of GST-HRV3C-His was demonstrated to be about 4500 U/mg and its application in the purification of another proteins carrying HRV3C-specific recognition sequence, LEVLFQ¯GP based on His-tag or GST-tag was also proved in this study.


2019 ◽  
Vol 103 (5) ◽  
pp. 2205-2216 ◽  
Author(s):  
Thi Khoa My Nguyen ◽  
Mi Ran Ki ◽  
Ryeo Gang Son ◽  
Seung Pil Pack

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