Image

HIGH-LEVEL SOLUBLE EXPRESSION OF THE FUNCTIONAL PEPTIDE DERIVED FROM THE C-TERMINAL DOMAIN OF THE OCEAN CUCUMBER LYSOZYME AND ANALYSIS OF ITS ANTIMICROBIAL ACTIVITY

Abstract

The sea cucumber lysozyme belongs to the family of invertebrate lysozymes and is believed to be a key defense considering protecting aquaculture animals against bacterial infection. Recently, evidence was found that the ocean cucumber lysozyme exerts broad-spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria, and it also has less attackable antimicrobial activity independent of its enzymatic activity. To explore the antimicrobial role of this non-enzymatic lysozyme and model its structure to novel antimicrobial peptides, the peptide from the C-terminal aminoalkanoic acid residues 70–146 of the ocean cucumber lysozyme in Stichopus japonicus (SjLys-C) was heterologously expressed in Escherichia coli Rosetta(DE3)pLysS.

Keywords
  • Affinity purificationLysozyme peptide molecular modelingRecombinant protein
References

Individual articles are published Open Access under the Creative Commons Licence: CC-BY 4.0.

How to Cite

PROF.DUHAOG, F.G; PROF.ZANG, P.J. MOONG, P. F. P. Z. P. M. (2021). HIGH-LEVEL SOLUBLE EXPRESSION OF THE FUNCTIONAL PEPTIDE DERIVED FROM THE C-TERMINAL DOMAIN OF THE OCEAN CUCUMBER LYSOZYME AND ANALYSIS OF ITS ANTIMICROBIAL ACTIVITY. International Journal of Multidisciplinary Research and Studies, 4(01). Retrieved from https://ijmras.com/index.php/ijmras/article/view/83

Download Citation

Downloads

Download data is not yet available.

Similar Articles

You may also start an advanced similarity search for this article.