2017
DOI: 10.1007/s13205-017-1056-3
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Antibiotic-free expression system for the production of human interferon-beta protein

Abstract: Recombinant human interferon-β (rhIFN-β), a therapeutic protein, is produced using both prokaryotic and eukaryotic expression systems. However, instability of recombinant plasmid during cultivation of results in low yield of the recombinant proteins. In addition, use of antibiotics during the cultivation imposes a major concern. In this study, we have compared the expression yield of rhIFN-β in BL21 (DE3) and SE1 cells. Gene-encoding rhIFN-β was expressed in BL21 (DE3) and SE1 cells and the cultivation of reco… Show more

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Cited by 6 publications
(2 citation statements)
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“…Hsp65-producing L. lactis in the present format is still not suitable for human use because of the antibiotic resistant gene and the requirement for xylose for Hsp65 induction. However, novel recombinant technologies that makes possible the expression of exogenous proteins in probiotics used for dairy products without the use of antibiotics and exogenous inducing agents are available ( 62 66 ). A version of Hsp65-producing L. lactis with such features would be suitable for clinical studies.…”
Section: Discussionmentioning
confidence: 99%
“…Hsp65-producing L. lactis in the present format is still not suitable for human use because of the antibiotic resistant gene and the requirement for xylose for Hsp65 induction. However, novel recombinant technologies that makes possible the expression of exogenous proteins in probiotics used for dairy products without the use of antibiotics and exogenous inducing agents are available ( 62 66 ). A version of Hsp65-producing L. lactis with such features would be suitable for clinical studies.…”
Section: Discussionmentioning
confidence: 99%
“…Images for the protein electrophoresis spectrum were taken using an AlphaEase FC gel imaging system (Genetic Technologies Inc, Miami, FL, USA). Densitometry analysis was performed using Image Studio Lite (version 5.2, LI-COR Biosciences, Lincoln, NE, USA) for the relative quantification of the different protein bands (66, 42, 39, 38, 27, 26, 22, and 18 kDa) …”
Section: Materials and Methodsmentioning
confidence: 99%