A novel acidic laminarinase derived from Jermuk hot spring metagenome.

ABSTRACT: Laminarinase, an enzyme with a specific affinity for laminarin-a complex polysaccharide found in the cell walls of brown algae and select marine organisms-was investigated in this study. We cloned and characterized a gene encoding a putative glycoside hydrolase family 16 (GH16) laminarinase derived from the Jermuk hot spring metagenome. The resulting product, named Jermuk-LamM, represents a novel 1,3-β-D-glucanase with 48.1% amino acid sequence similarity to previously characterized GH16 family members catalogued in the NCBI database. To date, this stands as the sole described endo-1,3-β-D-glucanase from the Fidelibacterota phylum, which was recently reclassified from Marinimicrobia. Jermuk-LamM, identified as an acidic laminarinase, exhibits optimal enzymatic activity at pH 5.0 and a temp

SUBMITTER: Paloyan A 

PROVIDER: S-EPMC12296878 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature