Exploring the Catalytic Mechanisms of a Newly Identified Salt-Activated Alginate Lyase from <i>Pseudoalteromonas carrageenovora</i> ASY5.

ABSTRACT: Alginate lyases are critical enzymes in hydrolyzing alginate into alginate oligosaccharides (AOS), which are bioactive compounds known for their antioxidant properties and ability to lower serum glucose and lipid concentrations. However, elucidating catalytic mechanisms and discovering enzymes with enhanced catalytic efficiency remain long-term challenges. Here, we report AlgL2491, a novel bifunctional and cold-adapted alginate lyase from Pseudoalteromonas carrageenovora ASY5, belonging to the polysaccharide lyase family 18. This enzyme uniquely cleaves both polyguluronic (polyG) and polymannuronic (polyM), predominantly releasing disaccharides, trisaccharides, and tetrasaccharides after 12 h of hydrolysis. The enzyme achieves peak catalytic efficiency at 35 °C and pH 7.5, with acti

SUBMITTER: Zhuang X 

PROVIDER: S-EPMC12193947 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature