Alpha13Glucanase

Alpha13glucanase is an enzyme that hydrolyzes alpha-1,3-glycosidic bonds in alpha-1,3-glucans, a polysaccharide component found in some fungal cell walls and related microbial glycoconjugates. The term alpha13glucanase may appear in databases or texts as a variant of the more common name alpha-1,3-glucanase; in the literature, these activities are typically described as alpha-1,3-glucanases or alpha-1,3-glucan hydrolases. The specific sequence, structure, and classification of a given alpha13glucanase can vary, and many such enzymes are secreted or cell-wall associated depending on the organism.

Biological role and occurrence: In fungi, alpha-1,3-glucan serves as a component of the cell wall that influences porosity and immune recognition. Alpha-1,3-glucanases can participate in remodeling the fungal wall, in sporulation or germination, and in antagonistic interactions such as mycoparasitism where a microbe degrades a competing fungal cell wall. In bacteria and other organisms, these enzymes may enable access to alpha-1,3-glucans as carbon sources or contribute to interactions with host organisms by modifying surface polysaccharides.

Biochemical properties: Enzymatic activity is specific for alpha-1,3-glycosidic bonds. Substrate preference, pH and temperature optima, and cofactor requirements vary with the enzyme’s source. Like other glycoside hydrolases, activity can be influenced by inhibitors or metal ions, and stability is commonly assessed under conditions relevant to the organism from which the enzyme is derived.

Applications and context: Potential uses include biocontrol of fungal pathogens, processing of fungal biomass, and basic research into fungal cell wall architecture. Given nomenclature variation, it is important to confirm the source and activity when encountering the term alpha13glucanase.