scholarly journals Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli.

1990 ◽  
Vol 172 (9) ◽  
pp. 4870-4876 ◽  
Author(s):  
B L Geller
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Electrochemical Potential ◽  
Membrane Bound

scholarly journals Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance

Catalysts ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 215
Author(s):  
Dan-Ping Zhang ◽  
Xiao-Ran Jing ◽  
An-Wen Fan ◽  
Huan Liu ◽  
Yao Nie ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Proteus Mirabilis ◽  
Binding Protein ◽  
Catalytic Efficiency ◽  
Maltose Binding Protein ◽  
Catalytic Performance ◽  
Cell Lysate ◽  
Active Expression ◽  
Membrane Bound

L-amino acid deaminases (LAADs) are membrane flavoenzymes that catalyze the deamination of neutral and aromatic L-amino acids to α-keto acids and ammonia. LAADs can be used to develop many important biotechnological applications. However, the transmembrane α-helix of LAADs restricts its soluble active expression and purification from a heterologous host, such as Escherichia coli. Herein, through fusion with the maltose-binding protein (MBP) tag, the recombinant E. coli BL21 (DE3)/pET-21b-MBP-PmLAAD was constructed and the LAAD from Proteus mirabilis (PmLAAD) was actively expressed as a soluble protein. After purification, the purified MBP-PmLAAD was obtained. Then, the catalytic activity of the MBP-PmLAAD fusion protein was determined and compared with the non-fused PmLAAD. After fusion with the MBP-tag, the catalytic efficiency of the MBP-PmLAAD cell lysate was much higher than that of the membrane-bound PmLAAD whole cells. The soluble MBP-PmLAAD cell lysate catalyzed the conversion of 100 mM L-phenylalanine (L-Phe) to phenylpyruvic acid (PPA) with a 100% yield in 6 h. Therefore, the fusion of the MBP-tag not only improved the soluble expression of the PmLAAD membrane-bound protein, but also increased its catalytic performance.

Expression of the murine leukemia virus protease in fusion with maltose-binding protein in Escherichia coli

2004 ◽  
Vol 35 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Anita Fehér ◽  
Péter Boross ◽  
Tamás Sperka ◽  
Stephen Oroszlan ◽  
József Tözsér
Keyword(s):  
Escherichia Coli ◽  
Murine Leukemia Virus ◽  
Binding Protein ◽  
Leukemia Virus ◽  
Maltose Binding Protein ◽  
Murine Leukemia
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