Xanthan lyase
Template:Infobox enzyme The enzyme xanthan lyase (Template:EnzExplorer) catalyzes the following process:
- Eliminative cleavage of the terminal β-D-mannosyl-(1→4)-β-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-α-L-threo-hex-4-enuronosyl group at the terminus of the side-chain
It belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Xanthan lyase was first identified and partially purified in 1987.[1]
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.[2] These side chains contain three monosaccharide residues. Xanthan lyase is produced by bacteria that degrade this polysaccharide, such as Bacillus, Corynebacterium, Bacteroides, Ruminococcaceae, and Paenibacillus species.[2][3][4]
Industrial applications
Xanthan is used in industry as a thickening agent in foods and drinks, as a stabilizing agent for foams, as a means of enhancing oil recovery and in the manufacture of good such as paints, cosmetics and explosives.[3] The use of xanthan lyase as a means of altering the physical properties of xanthans is an area of current research in biotechnology.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1J0M, 1J0N, 1X1H, 1X1I, 1X1J, 2E22, and 2E24. The enzyme from Bacillus is a monomer consisting of two domains: an alpha helical N-terminal domain, and a C-terminal domain composed of beta sheets.[5] The active site is a deep cleft located between these two domains.
References
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