Bovine lactoferricin B was successfully expressed as a fusion protein in E. coli with retained antimicrobial activity after cleavage — enabling cost-effective large-scale production of this antimicrobial peptide.
Key findingRecombinant bovine lactoferricin B expressed as a fusion protein in E. coli retained antimicrobial activity after enzymatic cleavage, establishing a s
What the researchers found
Recombinant bovine lactoferricin B expressed as a fusion protein in E. coli retained antimicrobial activity after enzymatic cleavage, establishing a scalable bacterial expression system for commercial antimicrobial peptide production.
Why it matters
Relevant for antimicrobial-peptides, peptide-design.
How the study worked
in-vitro study on antimicrobial-peptides, peptide-design.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2006.
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
Fusion expression of bovine lactoferricin in Escherichia coli.
Protein expression and purification, 47(1), 110-7
Citation
Feng, Xing-jun; Wang, Jian-hua; Shan, An-shan; Teng, Da; Yang, Ya-lin; Yao, Yi; Yang, Guan-pin; Shao, Yan-chun; Liu, Shuo; Zhang, Fan. (2006). Fusion expression of bovine lactoferricin in Escherichia coli.. Protein expression and purification, 47(1), 110-7.