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Item type:Publication, Access status: with files , A novel acidic laminarinase derived from Jermuk hot spring metagenome(Springer, 2025-07-26); ; ; ; 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 temperature of 55 °C, maintaining its function for a duration of at least 7 h. Jermuk-LamM is an enzyme that efficiently hydrolyzes both soluble and insoluble (1,3)-β-d-glucans, as well as (1,3;1,4)-β-d-glucans, with a marked preference for laminarin. This enzymatic activity facilitates the valorization of macroalgal biomass by predominantly producing monosaccharides and disaccharides. These hydrolysis products can subsequently be converted into energy carriers such as alcohol, methane, and hydrogen. The enzyme’s specific activities, coupled with its resistance to various additives, render Jermuk-LamM a promising candidate for various industrial applications, encompassing the realms of biofuel and pharmaceutical production. Key points: • Jermuk hot springs have significant potential as a source of novel enzymes. • Jermuk-LamM has less than 50% amino acid similarity to known enzymes. • It is the first enzyme characterized from the Fidelibacterota phylum.Publicationtype: Journal Article14 5 - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Access status: with files , Biodegradation of polyhydroxyalkanoates: current state and future prospects(Frontiers Media S.A., 2025); ; ; Polyhydroxyalkanoates (PHAs) are biobased and biodegradable polymers that offer a sustainable alternative to conventional plastics, addressing the escalating concerns over plastic pollution. While their environmental advantages are well-documented, the efficient degradation of PHAs in natural and engineered environments remains a critical component of their lifecycle. This review provides a comprehensive overview of PHA-degrading bacteria isolated from diverse ecosystems and highlights the pivotal role of PHA depolymerases in achieving PHA circularity. Microbial adaptation to diverse environmental conditions, such as extreme temperatures, salinity, and pH, significantly influences enzymes properties, including the stability, activity, and substrate specificity of PHA-degrading enzymes. These adaptations often enhance enzyme, performance, enabling functionality under challenging conditions. Consequently, extremophilic microorganisms are invaluable resources for discovering and engineering robust PHA depolymerases for industrial and environmental applications. This review underscores the urgent need for further research to improve the ecological and economic sustainability of PHA waste management.Publicationtype: Review Article6 14