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dc.creatorCong,Lina
dc.creatorLiang,Wenjing
dc.creatorWu,Yao
dc.creatorLi,Cheng
dc.creatorChang,Yihai
dc.creatorDong,Liang
dc.creatorSong,Wanlin
dc.creatorMa,Jun
dc.date2014-11-01
dc.date.accessioned2019-05-03T12:45:13Z
dc.date.available2019-05-03T12:45:13Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/85437
dc.descriptionBackground The sea cucumber lysozyme belongs to the family of invertebrate lysozymes and is thought to be a key defense factor in protecting aquaculture animals against bacterial infection. Recently, evidence was found that the sea cucumber lysozyme exerts broad spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria, and it also has more potent 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 amino acid residues 70-146 of the sea cucumber lysozyme in Stichopus japonicus (SjLys-C) was heterologously expressed in Escherichia coli Rosetta(DE3)pLysS. Results The fusion protein system led to over-expression of the soluble and highly stable product, an approximate 26 kDa recombinant SjLys-C protein (rSjLys-C). The present study showed that rSjLys-C displayed strong antimicrobial activity against the tested Gram-positive and Gram-negative bacteria. In particular, the heat-treated rSjLys-C exhibited more inhibitive activity than the native rSjLys-C. The structural analysis of SjLys-C showed that it is a typical hydrophilic peptide and contains a helix-loop-helix motif. The modeling of SjLys-C molecular structures at different temperatures revealed that the tertiary structure of SjLys-C at 100°C underwent a conformational change which is favorable for enhancing antimicrobial activity. Conclusion These results indicate that the expressed rSjLys-C is a highly soluble product and has a strong antimicrobial activity. Therefore, gaining a large quantity of biologically active rSjLys-C will be used for further biochemical and structural studies and provide a potential use in aquaculture and medicine.
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dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.relation10.1016/j.ejbt.2014.09.001
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.17 n.6 2014
dc.subjectAffinity purification
dc.subjectLysozyme peptide
dc.subjectMolecular modeling
dc.subjectRecombinant protein
dc.titleHigh-level soluble expression of the functional peptide derived from the C-terminal domain of the sea cucumber lysozyme and analysis of its antimicrobial activity


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