Expression of recombinant horseradish peroxidase C in Escherichia coli

1989 ◽  
Vol 17 (6) ◽  
pp. 1077-1078 ◽  
Author(s):  
JULIAN F. BURKE ◽  
ANDREW SMITH ◽  
NIOVI SANTAMA ◽  
ROBERT C. BRAY ◽  
ROGER N. F. THORNELEY ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Horseradish Peroxidase ◽  
Recombinant Horseradish Peroxidase

Characterization of Recombinant Horseradish Peroxidase C and three Site-Directed mutants, F41V, F41W, and R38K by Resonance Raman Spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (23) ◽  
pp. 7398-7407 ◽  
Author(s):  
Giulietta Smulevich ◽  
Mauro Paoli ◽  
Julian F. Burke ◽  
Andrew T. Smith ◽  
Stephen A. Sanders ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Horseradish Peroxidase ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Recombinant Horseradish Peroxidase

Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins

2000 ◽  
Vol 90 (6) ◽  
pp. 600-606 ◽  
Author(s):  
Akihiko Kondo ◽  
Jiro Kohda ◽  
Yasunori Endo ◽  
Tokuhisa Shiromizu ◽  
Yoichi Kurokawa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Horseradish Peroxidase

Studies on the Refolding Process of Recombinant Horseradish Peroxidase

2012 ◽  
Vol 54 (2) ◽  
pp. 484-492 ◽  
Author(s):  
Sedigheh Asad ◽  
Bahareh Dabirmanesh ◽  
Nasser Ghaemi ◽  
Seyed Masoud Etezad ◽  
Khosro Khajeh
Keyword(s):  
Horseradish Peroxidase ◽  
Recombinant Horseradish Peroxidase

scholarly journals Von der Wurzel ins Labor: Meerrettichperoxidase produziert in E. coli

BIOspektrum ◽  
2021 ◽  
Vol 27 (7) ◽  
pp. 773-775
Author(s):  
Julian Ebner ◽  
Diana Humer ◽  
Oliver Spadiut
Keyword(s):  
Escherichia Coli ◽  
Horseradish Peroxidase ◽  
Production Process ◽  
Inclusion Bodies ◽  
Medical Applications ◽  
Efficient Production ◽  
E Coli ◽  
Modern Biotechnology

AbstractThe enzyme Horseradish Peroxidase (HRP) is omnipresent in modern biotechnology. Although promising for therapeutic purposes, no suitable production process for this enzyme has been available until now. Medical applications require the enzyme to be highly pure, homogenous and well-defined. We have developed an efficient production process for recombinant HRP from Escherichia coli inclusion bodies. With this strategy we are able to provide active, highly pure and non-glycosylated enzyme at competitive yields.

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