Genomic and in silico protein structural analyses provide insights into marine polysaccharide-degrading enzymes in the sponge-derived Pseudoalteromonas sp. PA2MD11
Rodrigues de Oliveira, B.F.R.; Lopes, I.R.; Bauer Canellas, A.L.B.; Muricy, G.; Jackson, S.A.; Dobson, A.D.W.; 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: 973-995. https://dx.doi.org/10.1016/j.ijbiomac.2021.09.076
In: International Journal of Biological Macromolecules. ELSEVIER SCIENCE BV: Amsterdam. ISSN 0141-8130; e-ISSN 1879-0003, more
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| Keywords |
Plakina cyanorosea Muricy, Domingos, Lage, Lanna, Hardoim, Laport & Zilberberg, 2019 [WoRMS]
Marine/Coastal |
| Author keywords |
Agarase; Alginate lyase; Plakina cyanorosea; Sponge microbiome; Sulfatase |
| Authors | | Top |
- Rodrigues de Oliveira, B.F.R.
- Lopes, I.R.
- Bauer Canellas, A.L.B.
- Muricy, G.
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- Jackson, S.A.
- Dobson, A.D.W.
- Laport, M.S., more
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| Abstract |
Active 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 carbohydratedegrading 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 pharmacologicallyactive oligosaccharides. |
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