Identification of BgP, a cutinase-like polyesterase from a deep-sea sponge-derived actinobacterium

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dc.contributor.authorCarr, Clodagh M.
dc.contributor.authorRodrigues de Oliveira, Bruno Francesco
dc.contributor.authorJackson, Stephen A.
dc.contributor.authorLaport, Marinella Silva
dc.contributor.authorClarke, David J.
dc.contributor.authorDobson, Alan D. W.
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderFundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiroen
dc.contributor.funderConselho Nacional de Desenvolvimento Científico e Tecnológicoen
dc.date.accessioned2022-05-13T10:45:40Z
dc.date.available2022-05-13T10:45:40Z
dc.date.issued2022-04-12
dc.date.updated2022-05-13T10:37:00Z
dc.description.abstractMany marine bacteria produce extracellular enzymes that degrade complex molecules to facilitate their growth in environmental conditions that are often harsh and low in nutrients. Marine bacteria, including those inhabiting sea sponges, have previously been reported to be a promising source of polyesterase enzymes, which have received recent attention due to their potential ability to degrade polyethylene terephthalate (PET) plastic. During the screening of 51 marine bacterial isolates for hydrolytic activities targeting ester and polyester substrates, a Brachybacterium ginsengisoli B129SM11 isolate from the deep-sea sponge Pheronema sp. was identified as a polyesterase producer. Sequence analysis of genomic DNA from strain B129SM11, coupled with a genome "mining" strategy, allowed the identification of potential polyesterases, using a custom database of enzymes that had previously been reported to hydrolyze PET or other synthetic polyesters. This resulted in the identification of a putative PET hydrolase gene, encoding a polyesterase-type enzyme which we named BgP that shared high overall similarity with three well-characterized PET hydrolases-LCC, TfCut2, and Cut190, all of which are key enzymes currently under investigation for the biological recycling of PET. In silico protein analyses and homology protein modeling offered structural and functional insights into BgP, and a detailed comparison with Cut190 revealed highly conserved features with implications for both catalysis and substrate binding. Polyesterase activity was confirmed using an agar-based polycaprolactone (PCL) clearing assay, following heterologous expression of BgP in Escherichia coli. This is the first report of a polyesterase being identified from a deep-sea sponge bacterium such as Brachybacterium ginsengisoli and provides further insights into marine-derived polyesterases, an important family of enzymes for PET plastic hydrolysis. Microorganisms living in association with sponges are likely to have increased exposure to plastics and microplastics given the wide-scale contamination of marine ecosystems with these plastics, and thus they may represent a worthwhile source of enzymes for use in new plastic waste management systems. This study adds to the growing knowledge of microbial polyesterases and endorses further exploration of marine host-associated microorganisms as a potentially valuable source of this family of enzymes for PET plastic hydrolysis.en
dc.description.sponsorshipScience Foundation Ireland (SFI grant numbers: 12/RC/2275_2); Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (E-26/200.948/2021; E-26/202.144/2020; E-26/211.284/2021); Conselho Nacional de Desenvolvimento Científico e Tecnológico (306395/2020-7).en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid888343en
dc.identifier.citationCarr, C. M., Rodrigues de Oliveira, B. F., Jackson, S. A., Laport, M. S., Clarke, D. J. and Dobson, A. D. W. (2022) 'Identification of BgP, a cutinase-like polyesterase from a deep-sea sponge-derived actinobacterium', Frontiers in Microbiology, 13, 888343 (16pp). doi: 10.3389/fmicb.2022.888343en
dc.identifier.doi10.3389/fmicb.2022.888343en
dc.identifier.eissn1664-302X
dc.identifier.endpage16en
dc.identifier.journaltitleFrontiers in Microbiologyen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/13177
dc.identifier.volume13en
dc.language.isoenen
dc.publisherFrontiers Media S.A.en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2275/IE/Synthesis and Solid State Pharmaceutical Centre (SSPC)/en
dc.rights© 2022, Carr, de Oliveira, Jackson, Laport, Clarke and Dobson. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original authors and the copyright owners are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectPolyesteraseen
dc.subjectCutinaseen
dc.subjectPETaseen
dc.subjectPlasticen
dc.subjectMarineen
dc.titleIdentification of BgP, a cutinase-like polyesterase from a deep-sea sponge-derived actinobacteriumen
dc.typeArticle (peer-reviewed)en
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