Analysis for residual host cell proteins and DNA in process streams of a recombinant protein product expressed in Escherichia coli cells

2003 ◽  
Vol 32 (6) ◽  
pp. 1199-1211 ◽  
Author(s):  
Anurag Singh Rathore ◽  
S.E. Sobacke ◽  
T.J. Kocot ◽  
D.R. Morgan ◽  
R.L. Dufield ◽  
...  
2016 ◽  
Vol 11 (9) ◽  
pp. 1934578X1601100 ◽  
Author(s):  
Takahiro Kato ◽  
Jung-Bum Lee ◽  
Futoshi Taura ◽  
Fumiya Kurosaki

Two genes involved in δ-guaiene biosynthesis in Aquilaria microcarpa, δ-guaiene synthase (GS) and farnesyl diphosphate synthase (FPS), were overexpressed in Escherichia coli cells. Immunoblot analysis revealed that the concentration of GS-translated protein was rather low in the cells transformed by solely GS while appreciable accumulation of the recombinant protein was observed when GS was coexpressed with FPS GS-transformed cells liberated only a trace amount of δ-guaiene (0.004 μg/mL culture), however, the concentration of the compound elevated to 0.08 μg/mL culture in the cells transformed by GS plus FPS δ-Guaiene biosynthesis was markedly activated when E. coli cells coexpressing GS and FPS were incubated in enriched Terrific broth, and the content of the compound increased to approximately 0.6 μg/mL culture. These results suggest that coexpression of FPS and GS in E. coli is required for efficient 6-guaiene production in the bacterial cells, and the sesquiterpene-producing activity of the transformant is appreciably enhanced in the nutrients-enriched medium.


1991 ◽  
Vol 55 (3) ◽  
pp. 743-750 ◽  
Author(s):  
Masaharu KANAOKA ◽  
Takaharu NEGORO ◽  
Chigusa KAWANAKA ◽  
Hideo AGUI ◽  
Shigeyasu NABESHIMA

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