Fucanases Related to the GH107 Family from Members of the PVC Superphylum

PONCE, NORA M. A.; STORTZ, CARLOS A.; LOZADA, MARIANA; DIONISI, HEBE M.; GONZALEZ, JESSICA A.; DAGLIO, YASMÍN

Journal of Marine Science and Engineering

MDPI

Año: 2024 vol. 12

The glycoside hydrolase 107 (GH107) family includes fucanase enzymes from only two bac-terial phyla, Bacteroidota and Pseudomonadota. The goal of this work was to explore the diversity ofputative fucanase enzymes related to this family in organisms of the PVC superphylum (Planctomyce-tota, Verrucomicrobiota, Chlamydiota), in order to expand our knowledge of the fucoidan-degradingpotential in this ecologically and biotechnologically relevant group. Using hidden Markov model-and peptide-based annotation tools, 26 GH107 homolog sequences were identified in metagenomeand genome datasets. The sequences formed two distinct clusters in a phylogenetic analysis, only oneincluding members of the GH107 family. The endo-acting fucoidan degrading activity was confirmedin an enzyme included in the most divergent cluster. The fucanase, which probably originated in anuncultured planctomycete from the sampled subantarctic sediments, was cloned and expressed inEscherichia coli. The enzyme catalyzed the rapid hydrolysis of internal glycosidic bonds of fucoidanfrom Macrocystis pyrifera, a macroalgae species abundant at the site. It was active in a wide rangeof temperatures (5–45 ◦ C), salinities (9.5–861 mM NaCl), and pH values (4.5–9), mainly producingsulfated α-(1,3)-linked fuco-oligosaccharides of various lengths. The PVC superphylum represents apromising source of fucanase enzymes with various biotechnological applications.