Genomic and in silico protein structural analyses provide insights into marine polysaccharide-degrading enzymes in the sponge-derived Pseudoalteromonas sp. PA2MD11

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dc.contributor.authorde Oliveira, Bruno Francesco Rodrigues
dc.contributor.authorRodrigues Lopes, Isabelle
dc.contributor.authorBauer Canellas, Anna Luiza
dc.contributor.authorMuricy, Guilherme
dc.contributor.authorJackson, Stephen Anthony
dc.contributor.authorDobson, Alan D. W.
dc.contributor.authorLaport, Marinella Silva
dc.contributor.funderFundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiroen
dc.contributor.funderCoordenação de Aperfeiçoamento de Pessoal de Nível Superioren
dc.contributor.funderConselho Nacional de Desenvolvimento Científico e Tecnológicoen
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2021-10-18T11:11:28Z
dc.date.available2021-10-18T11:11:28Z
dc.date.issued2021-09-21
dc.date.updated2021-10-18T10:35:36Z
dc.description.abstractActive heterotrophic metabolism is a critical metabolic role performed by sponge-associated microorganisms, but little is known about their capacity to metabolize marine polysaccharides (MPs). Here, we investigated the genome of the sponge-derived Pseudoalteromonas sp. strain PA2MD11 focusing on its macroalgal carbohydrate-degrading potential. Carbohydrate-active enzymes (CAZymes) for the depolymerization of agar and alginate were found in PA2MD11's genome, including glycoside hydrolases (GHs) and polysaccharide lyases (PLs) belonging to families GH16, GH50 and GH117, and PL6 and PL17, respectively. A gene potentially encoding a sulfatase was also identified, which may play a role in the strain's ability to consume carrageenans. The complete metabolism of agar and alginate by PA2MD11 could also be predicted and was consistent with the results obtained in physiological assays. The polysaccharide utilization locus (PUL) potentially involved in the metabolism of agarose contained mobile genetic elements from other marine Gammaproteobacteria and its unusual larger size might be due to gene duplication events. Homology modelling and structural protein analyses of the agarases, alginate lyases and sulfatase depicted clear conservation of catalytic machinery and protein folding together with suitable industrially-relevant features. Pseudoalteromonas sp. PA2MD11 is therefore a source of potential MP-degrading biocatalysts for biorefinery applications and in the preparation of pharmacologically-active oligosaccharides.en
dc.description.sponsorshipFundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) (Grant numbers E-26/203.320/2017; E-26/201.814/2018; E-26/202.898/2018; E-26/211.554/2019; E-26/202.144/2020); Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) (Grant numbers Finance Code 001, 88887.341847/2019-00); Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) (Grant numbers 140840/2018-4; 152901/2019-1; 306395/2020-7); Science Foundation Ireland (Grant numbers SSPC-3 12/RC/2275_2; SSPC-2, 12/RC/ 2275)en
dc.description.statusPeer revieweden
dc.description.versionAccepted Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationde Oliveira, B. F. R., Rodrigues Lopes, I., Bauer Canellas, A. L., Muricy, G., Jackson, S. A., Dobson, A. D. W. and Laport, M. S. (2021) 'Genomic and in silico protein structural analyses provide insights into marine polysaccharide-degrading enzymes in the sponge-derived Pseudoalteromonas sp. PA2MD11', International Journal of Biological Macromolecules, 191, pp. 973-995. doi: 10.1016/j.ijbiomac.2021.09.076en
dc.identifier.doi10.1016/j.ijbiomac.2021.09.076en
dc.identifier.endpage995en
dc.identifier.issn0141-8130
dc.identifier.journaltitleInternational Journal of Biological Macromoleculesen
dc.identifier.startpage973en
dc.identifier.urihttps://hdl.handle.net/10468/12108
dc.identifier.volume191en
dc.language.isoenen
dc.rights© 2021, Elsevier B.V. All rights reserved. This manuscript version is made available under the CC BY-NC-ND 4.0 license.en
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectAgaraseen
dc.subjectAlginate lyaseen
dc.subjectPlakina cyanoroseaen
dc.subjectSponge microbiomeen
dc.subjectSulfataseen
dc.titleGenomic and in silico protein structural analyses provide insights into marine polysaccharide-degrading enzymes in the sponge-derived Pseudoalteromonas sp. PA2MD11en
dc.typeArticle (peer-reviewed)en
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