scholarly journals Characterization of In Vitro Interactions between a Truncated TonB Protein from Escherichia coli and the Outer Membrane Receptors FhuA and FepA

2001 ◽  
Vol 183 (9) ◽  
pp. 2755-2764 ◽  
Author(s):  
G. S. Moeck ◽  
L. Letellier
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Receptors ◽  
Tonb Protein ◽  
In Vitro Interactions

scholarly journals In vitro folding, purification and characterization of Escherichia coli outer membrane protease OmpT

2000 ◽  
Vol 267 (3) ◽  
pp. 885-893 ◽  
Author(s):  
R. A. Kramer ◽  
Davika Zandwijken ◽  
Maarten R. Egmond ◽  
Niek Dekker
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Purification And Characterization

scholarly journals Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

2021 ◽  
Vol 7 (5) ◽  
pp. 325
Author(s):  
Laura Isabel de de Eugenio ◽  
Rosa Peces-Pérez ◽  
Dolores Linde ◽  
Alicia Prieto ◽  
Jorge Barriuso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Inclusion Bodies ◽  
Veratryl Alcohol ◽  
Dye Decolorization ◽  
Irpex Lacteus ◽  
Type D ◽  
Lignin Peroxidases

A dye-decolorizing peroxidase (DyP) from Irpex lacteus was cloned and heterologously expressed as inclusion bodies in Escherichia coli. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol (DMP), and anthraquinoid and azo dyes as reported for other fungal DyPs, but it was also able to oxidize Mn2+ (as manganese peroxidases and versatile peroxidases) and veratryl alcohol (VA) (as lignin peroxidases and versatile peroxidases). This corroborated that I. lacteus DyPs are the only enzymes able to oxidize high redox potential dyes, VA and Mn+2. Phylogenetic analysis grouped this enzyme with other type D-DyPs from basidiomycetes. In addition to its interest for dye decolorization, the results of the transformation of softwood and hardwood lignosulfonates suggest a putative biological role of this enzyme in the degradation of phenolic lignin.

In vitro functional characterization of overproduced Escherichia coli katF/rpoS gene product

Biochemistry ◽  
1993 ◽  
Vol 32 (41) ◽  
pp. 11112-11117 ◽  
Author(s):  
Lam H. Nguyen ◽  
Debra B. Jensen ◽  
Nancy E. Thompson ◽  
Daniel R. Gentry ◽  
Richard R. Burgess
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
Functional Characterization ◽  
Rpos Gene
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