Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase

1997 ◽  
Vol 47 (4) ◽  
pp. 373-378 ◽  
Author(s):  
N. Sriubolmas ◽  
W. Panbangred ◽  
S. Sriurairatana ◽  
V. Meevootisom
Keyword(s):  
Escherichia Coli ◽  
Inclusion Bodies ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Escherichia Coli Cells

Periplasmic penicillin G acylase activity in recombinant Escherichia coli cells permeabilized with organic solvents

2003 ◽  
Vol 39 (3) ◽  
pp. 301-305 ◽  
Author(s):  
A. De León ◽  
B. Garcı́a ◽  
A.P. Barba de la Rosa ◽  
F. Villaseñor ◽  
A. Estrada ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Organic Solvents ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Escherichia Coli Cells

Optimization of the host–plasmid interaction in the recombinant Escherichia coli strains overproducing penicillin G acylase

2004 ◽  
Vol 35 (1) ◽  
pp. 74-80 ◽  
Author(s):  
Renata Valešová ◽  
Lenka Hollerová-Sobotková ◽  
Václav Štěpánek ◽  
Pavel Kyslı́k
Keyword(s):  
Escherichia Coli ◽  
Recombinant Escherichia Coli ◽  
Penicillin G Acylase ◽  
Penicillin G

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.

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