In silico screening and heterologous expression of a Polyethylene Terephthalate hydrolase (PETase)- like enzyme (SM14est) with Polycaprolactone (PCL)-degrading activity, from the marine sponge-derived strain Streptomyces sp. SM14.

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dc.contributor.authorAlmeida, Eduardo L.
dc.contributor.authorRincón, Andrés Felipe Carrillo
dc.contributor.authorJackson, Stephen A.
dc.contributor.authorDobson, Alan D. W.
dc.contributor.funderConselho Nacional de Desenvolvimento Científico e Tecnológicoen
dc.contributor.funderMarine Instituteen
dc.contributor.funderJiangsu Key Laboratory of Marine Biotechnologyen
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2019-10-14T21:57:12Z
dc.date.available2019-10-14T21:57:12Z
dc.date.issued2019-10-01
dc.description.abstractPlastics, such as the polyethylene terephthalate (PET), are widely used for various industrial applications, due to their physicochemical properties which are particularly useful in the packaging industry. However, due to improper plastic waste management and difficulties in recycling, post-consumer plastic waste has become a pressing issue for both the environment and for human health. Hence, novel technologies and methods of processing plastic waste are required to address these issues. Enzymatic-assisted hydrolysis of synthetic polymers has been proposed as a potentially more efficient and environment-friendly alternative to the currently employed methods. Recently, a number of PET hydrolases have been described, and in particular a PETase derived from Ideonella sakaiensis 201-F6 (IsPETase), which appears to be the most efficient and substrate-specific bacterial PET hydrolase enzyme discovered to date. In order to further investigate this class of PETase-like enzymes, we employed an in silico-based screening approach on the biotechnologically relevant genus Streptomyces, including terrestrial and marine isolates; in a search for potential PETase homologs. From a total of 52 genomes analyzed, we were able to identify three potential PETase-like enzymes, all of which were derived from marine-sponge associated Streptomyces isolates. A candidate PETase-like gene (SM14est) was identified in Streptomyces sp. SM14. Further in silico characterization of the SM14est protein sequence and its predicted three-dimensional structure were performed and compared to the well-characterized IsPETase. Both the serine hydrolase motif Gly-x1-Ser-x2-Gly and the catalytic triad Ser, Asp, His are conserved in both sequences. Molecular docking experiments indicated that the SM14est enzyme possessed the capacity to bind plastics as substrates. Finally, polyesterase activity was confirmed using a polycaprolactone (PCL) plate clearing assay which is a model substrate for the degradation of plastics; following heterologous expression of SM14est in Escherichia coli, with secretion being facilitated by the native Streptomyces signal peptide. These findings provide further insights into this important class of PETase-like enzymes.en
dc.description.sponsorshipScience Foundation Ireland (SSPC-2); Marine Biotechnology ERA/NET (NEPTUNA project contract no. PBA/MB/15/02); Marine Institute (NMBLI project Grant-Aid Agreement PBA/MB/16/01)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid2187en
dc.identifier.citationAlmeida, E. L., Rincón, A. F. C., Jackson, S. A. and Dobson, A. D. W. (2019) 'In silico Screening and Heterologous Expression of a Polyethylene Terephthalate Hydrolase (PETase)-Like Enzyme (SM14est) With Polycaprolactone (PCL)-Degrading Activity, From the Marine Sponge-Derived Strain Streptomyces sp. SM14', Frontiers in Microbiology, 10, 2187. (14pp.) DOI: 10.3389/fmicb.2019.02187en
dc.identifier.doi10.3389/fmicb.2019.02187en
dc.identifier.eissn1664-302X
dc.identifier.endpage14en
dc.identifier.journaltitleFrontiers in Microbiologyen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/8758
dc.identifier.volume10en
dc.language.isoenen
dc.publisherFrontiers Mediaen
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2275/IE/Synthesis and Solid State Pharmaceutical Centre (SSPC)/en
dc.rights©2019 Almeida, Carrillo Rincón, Jackson 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 author(s) and the copyright owner(s) 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.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectPETaseen
dc.subjectMarine sponge associated bacteriaen
dc.subjectHeterologous protein expressionen
dc.subjectPolycaprolactone (PCL)en
dc.subjectSynthetic polyestersen
dc.titleIn silico screening and heterologous expression of a Polyethylene Terephthalate hydrolase (PETase)- like enzyme (SM14est) with Polycaprolactone (PCL)-degrading activity, from the marine sponge-derived strain Streptomyces sp. SM14.en
dc.typeArticle (peer-reviewed)en
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