Improvement in extracellular secretion of recombinant L-asparaginase II by Escherichia coli BL21 (DE3) using glycine and n-dodecane. [PDF]
Flores-Santos JC +4 more
europepmc +1 more source
Cloning, Expression and Evaluation of Pseudomonas Aeruginosa Exotoxin A
Background: Nowadays, in many studies related to the treatment of various cancers, toxic compounds are targeted against cancer cells. One of the most effective compounds is Pseudomonas exotoxin A.
Jahangir Langari +6 more
doaj
Refolding of bioactive human epidermal growth factor from E. coli BL21(DE3) inclusion bodies & evaluations on its in vitro & in vivo bioactivity. [PDF]
Maksum IP +5 more
europepmc +1 more source
Optimization of haloacid dehalogenase production by recombinant E. coli BL21 (DE3)/pET-hakp1 containing haloacid dehalogenase gene from Klebsiella pneumoniae ITB1 using Response Surface Methodology (RSM). [PDF]
Ratnaningsih E +4 more
europepmc +1 more source
Safety of 3'-sialyllactose (3'-SL) sodium salt produced by derivative strains of Escherichia coli BL21 (DE3) as a Novel Food pursuant to Regulation (EU) 2015/2283. [PDF]
EFSA Panel on Nutrition +28 more
europepmc +1 more source
Large-Scale Preparation of Highly Stable Recombinant Human Acidic Fibroblast Growth Factor in Escherichia coli BL21(DE3) plysS Strain. [PDF]
Yu B +10 more
europepmc +1 more source
Título en ingles: Expression and purification of rotavirus structural proteins VP5* and VP8* in bacteria E. coli BL21(DE3) Resumen La caracterización de las proteínas estructurales del rotavirus y de las proteínas de la superficie de la célula hospedera ...
Luz Yurany Moreno +2 more
doaj
Disrupting ribulose-5-phosphate metabolic flux enhances riboflavin production in Escherichia coli BL21(DE3). [PDF]
Ying J +6 more
europepmc +1 more source
Optimization of a T7-RNA polymerase system in Synechococcus sp. PCC 7002 mirrors the protein overproduction phenotype from E. coli BL21(DE3). [PDF]
Jones CM +3 more
europepmc +1 more source
Aim: Plastic pollution caused by the persistence of polyethylene terephthalate (PET) has become a major environmental challenge due to its resistance to natural degradation. Biocatalytic degradation using PETase provides an eco-friendly and sustainable solution for PET recycling.
openaire +2 more sources

