Show simple item record

dc.contributor.authorSun, Baode
dc.contributor.authorWibowo, David
dc.contributor.authorMiddelberg, Anton PJ
dc.contributor.authorZhao, Chun-Xia
dc.date.accessioned2019-05-29T12:43:03Z
dc.date.available2019-05-29T12:43:03Z
dc.date.issued2018
dc.identifier.issn2191-0855
dc.identifier.doi10.1186/s13568-018-0541-3
dc.identifier.urihttp://hdl.handle.net/10072/370794
dc.description.abstractAntimicrobial peptides (AMPs) have significant potential as alternatives to classical antibiotics. However, AMPs are currently prepared using processes which are often laborious, expensive and of low-yield, thus hindering their research and application. Large-scale methods for production of AMPs using a cost-effective approach is urgently required. In this study, we report a scalable, chromatography-free downstream processing method for producing an antimicrobial peptide, pexiganan, using recombinant Escherichia coli (E. coli). The four helix bundle structure of the unique carrier protein DAMP4 was used to facilitate a simple and cheap purification process based on a selective thermochemical precipitation. Highly pure fusion protein DAMP4var-pexiganan was obtained at high yield (around 24 mg per 800 mL cell culture with a final cultivation OD600 ~ 2). The purification yield of DAMP4var-pexiganan protein is increased twofold with a 72.9% of the protein recovery in this study as compared to the previous purification processes (Dwyer in Chem Eng Sci 105:12–21, 2014). The antimicrobial peptide pexiganan was released and activated from the fusion protein by a simple acid-cleavage. Isoelectric precipitation was then applied to separate the pexiganan peptide from the DAMP4var protein carrier. The final yield of pure bio-produced pexiganan was 1.6 mg from 800 mL of bacterial cell culture (final cultivation OD600 ~ 2). The minimum bactericidal concentration (MBC) test demonstrated that the bio-produced pexiganan has the same antimicrobial activity as chemically synthesized counterpart. This novel downstream process provides a new strategy for simple and probable economic production of antimicrobial peptides.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer
dc.publisher.placeGermany
dc.relation.ispartofchapter6
dc.relation.ispartofpagefrom1
dc.relation.ispartofpageto14
dc.relation.ispartofjournalAMB Express
dc.relation.ispartofvolume8
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchMicrobiology not elsewhere classified
dc.subject.fieldofresearchChemical engineering
dc.subject.fieldofresearchcode3107
dc.subject.fieldofresearchcode310799
dc.subject.fieldofresearchcode4004
dc.titleCost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© The Author(s) 2018. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
gro.hasfulltextFull Text
gro.griffith.authorWibowo, David


Files in this item

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record