Xanthan Lyase

In enzymology, a xanthan lyase (EC 4.2.2.12) is an enzyme that catalyzes the chemical reaction of cleaving the beta-D-mannosyl-beta-D-1,4-glucuronosyl bond on the polysaccharide xanthan. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Xanthan lyase was first identified and partially purified in 1987.

Xanthan is a polysaccharide secreted by several different bacterial taxa, such as the plant pathogen Xanthomonas campestris, and it consists of a main linear chain based on cellulose with side chains attached to alternate glucosyl (glucose) residues. These side chains contain three monosaccharide residues. Xanthan lyase is produced by bacteria that degrade this polysaccharide, such as Bacillus, Corynebacterium and Paenibacillus species.