Insights into putative alginate lyases from epipelagic and mesopelagic communities of the global ocean.

Alginate lyases and oligoalginate lyases catalyze the cleavage of the glycosidic bonds of alginate, an acidic polysaccharide synthesized by brown algae and other organisms. These enzymes are highly diverse, currently classified into 15 families of the Carbohydrate-Active Enzyme (CAZy) database. We explored the structural and taxonomic diversity, the biogeographic distribution of the genes and transcripts, and the potential environmental drivers of putative alginate-degrading enzymes from picoplanktonic communities of the upper layers of the global ocean. The identified sequences were first analyzed using sequence similarity networks to assess their relationship with CAZy members. Sequences related to the PL5, PL6, PL7, PL17, and PL38 families had higher gene and transcript abundances, with temperature being a key driver of the structuring of the community members carrying putative alginate lyase genes. PL5 homologs included variants in a key residue of the active site, and sequences assigned to 'Candidatus Pelagibacter' showed high gene and transcript abundances that negatively correlated with inorganic phosphorus concentrations. Sequences assigned to Flavobacteriia and/or Gammaproteobacteria classes dominated the PL6, PL7, and PL17 families, in particular those closely related to sequences from uncultured Polaribacter and Alteromonas australica. In the PL38 family, while sequences assigned to taxa from the Planctomycetota, Verrucomicrobiota, and Bacteroidota phyla showed the highest relative gene abundance at most regions and depths, high expression levels were observed at high latitudes in sequences assigned to Eukaryota (e.g., Phaeocystis antarctica). Overall, the putative enzymes uncovered in this study could be involved in various physiological processes, including alginate assimilation and biosynthesis.