Goat lactoferricin was expressed in E. coli with retained antibacterial activity, expanding the species sources for recombinant lactoferricin production beyond bovine and human variants.
Key findingGoat lactoferricin cloned and expressed in E. coli AD494(DE3)pLysS with retained antibacterial activity against test organisms, expanding the recombin
What the researchers found
Goat lactoferricin cloned and expressed in E. coli AD494(DE3)pLysS with retained antibacterial activity against test organisms, expanding the recombinant lactoferricin production to a third species source.
Why it matters
Relevant for antimicrobial-peptides, peptide-design.
How the study worked
in-vitro study.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2008.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Cloning and expression of antibacterial goat lactoferricin from Escherichia coli AD494(DE3)pLysS expression system.
Journal of food protection, 71(12), 2523-5
Citation
Chen, Gen-Hung; Yin, Li-Jung; Chiang, I-Hua; Jiang, Shann-Tzong. (2008). Cloning and expression of antibacterial goat lactoferricin from Escherichia coli AD494(DE3)pLysS expression system.. Journal of food protection, 71(12), 2523-5.