Development of fenitrothion adsorbing recombinant Escherichia coli by cell surface display of pesticide-binding peptide

2020 ◽  
Vol 322 ◽  
pp. 90-95
Author(s):  
Yuanyuan Wang ◽  
Murali Kannan Maruthamuthu ◽  
Jaehoon Jeong ◽  
Ik-Keun Yoo ◽  
Tae Wan Kim ◽  
...  
2017 ◽  
Vol 41 (4) ◽  
pp. 479-487 ◽  
Author(s):  
Murali kannan Maruthamuthu ◽  
Jiyeon Hong ◽  
Kulandaisamy Arulsamy ◽  
Sivachandiran Somasundaram ◽  
SoonHo Hong ◽  
...  

AMB Express ◽  
2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Meisam Jeiranikhameneh ◽  
Mohamad Reza Razavi ◽  
Shiva Irani ◽  
Seyed Davar Siadat ◽  
Mana Oloomi

2012 ◽  
Vol 78 (9) ◽  
pp. 3051-3058 ◽  
Author(s):  
Hyeok-Jin Ko ◽  
Eunhye Park ◽  
Joseph Song ◽  
Taek Ho Yang ◽  
Hee Jong Lee ◽  
...  

ABSTRACTAutotransporters have been employed as the anchoring scaffold for cell surface display by replacing their passenger domains with heterologous proteins to be displayed. We adopted an autotransporter (YfaL) ofEscherichia colifor the cell surface display system. The critical regions in YfaL for surface display were identified for the construction of a ligation-independent cloning (LIC)-based display system. The designed system showed no detrimental effect on either the growth of the host cell or overexpressing heterologous proteins on the cell surface. We functionally displayed monomeric red fluorescent protein (mRFP1) as a reporter protein and diverse agarolytic enzymes fromSaccharophagus degradans2-40, including Aga86C and Aga86E, which previously had failed to be functional expressed. The system could display different sizes of proteins ranging from 25.3 to 143 kDa. We also attempted controlled release of the displayed proteins by incorporating a tobacco etch virus protease cleavage site into the C termini of the displayed proteins. The maximum level of the displayed protein was 6.1 × 104molecules per a single cell, which corresponds to 5.6% of the entire cell surface of actively growingE. coli.


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