Characterization of a novel immobilized biocatalyst obtained by matrix-assisted refolding of recombinant polyhydroxyoctanoate depolymerase from Pseudomonas putida KT2442 isolated from inclusion bodies

2010 ◽  
Vol 38 (9) ◽  
pp. 1203-1209 ◽  
Author(s):  
M. Arroyo ◽  
J. García-Hidalgo ◽  
M. Villalón ◽  
L. de Eugenio ◽  
D. Hormigo ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Inclusion Bodies ◽  
Immobilized Biocatalyst

Refolding, purification, and characterization of constitutive-active human-Smad8 produced as inclusion bodies in ClearColi® BL21 (DE3)

2021 ◽  
Vol 184 ◽  
pp. 105878
Author(s):  
Carla Lizbeth Segovia-Trinidad ◽  
Bastian Quaas ◽  
Zhaopeng Li ◽  
Antonina Lavrentieva ◽  
Yvonne Roger ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
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.

Characterization of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida.

1998 ◽  
Vol 62 (3) ◽  
pp. 469-478 ◽  
Author(s):  
Osao ADACHI ◽  
Tatsuro KUBOTA ◽  
Ayse HACISALIHOGLU ◽  
Hirohide TOYAMA ◽  
Emiko SHINAGAWA ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Amine Dehydrogenase

Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4

2010 ◽  
Vol 101 (19) ◽  
pp. 7516-7522 ◽  
Author(s):  
Wenjing Shen ◽  
Weidong Liu ◽  
Jing Zhang ◽  
Jian Tao ◽  
Haihua Deng ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Gene Cluster

scholarly journals Characterization of ligand response properties of the CRP protein from Pseudomonas putida

2012 ◽  
Vol 57 (30) ◽  
pp. 3878-3885 ◽  
Author(s):  
Feng Jiang ◽  
ZheXian Tian ◽  
YiPing Wang
Keyword(s):  
Pseudomonas Putida ◽  
Response Properties
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