Lichenase
class of enzymes
Lichenase (EC 3.2.1.73), also known as licheninase or 1,3-1,4 ꞵ-D-glucanase, is an enzyme that hydrolyzes the β-1,4 glycosidic bond next to the β-1,3 bond in the polysaccharides lichenin and β-glucan. These polysaccharides are found in the cell walls of lichens and grains, respectively. In Bacillus species, lichenase is produced by the licA gene. Lichenase is a hydrolase, which means it uses water to cleave bonds. Specifically, lichenase is a glycosidase, or an enzyme that hydrolyzes O- and S-glycosyl compounds.
Activity
Lichenase breaks the β-1,4 glycosidic bonds next to the β-1,3 bonds in mixed-linkage β-glucans in a reaction using water, known as hydrolysis. This is a double-displacement reaction, where a β-glucan combines with a water molecule and produces two products of either trisaccharides or tetrasaccharides. In Bacillus subtilis, these products are the oligosaccharides cellobiosyltriose and cellotriosyltetraose. These intermediary sugars can then be broken down further in order to produce energy for the organism. Lichenase performs differently from other β-glucanases, such as laminarinase and cellulase, due to its specificity in the bonds that it breaks, while the other β-glucanases act on bonds in other configurations.
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This entry incorporates text from “Lichenase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.