The enzyme xanthan lyase (EC 4.2.2.12) catalyzes the following process:
| xanthan lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.2.12 | ||||||||
| CAS no. | 113573-69-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- 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
editXanthan 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
editAs 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
edit- ^ Sutherland IW (1987). "Xanthan lyases--novel enzymes found in various bacterial species". J. Gen. Microbiol. 133 (11): 3129–34. doi:10.1099/00221287-133-11-3129. PMID 3446747.
- ^ a b Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K (1 October 1998). "Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains". Appl. Environ. Microbiol. 64 (10): 3765–8. Bibcode:1998ApEnM..64.3765H. doi:10.1128/AEM.64.10.3765-3768.1998. PMC 106543. PMID 9758797.
- ^ a b Ruijssenaars HJ, de Bont JA, Hartmans S (1 June 1999). "A pyruvated mannose-specific xanthan lyase involved in xanthan degradation by Paenibacillus alginolyticus XL-1". Appl. Environ. Microbiol. 65 (6): 2446–52. Bibcode:1999ApEnM..65.2446R. doi:10.1128/AEM.65.6.2446-2452.1999. PMC 91360. PMID 10347025.
- ^ Ostrowski, Matthew P.; La Rosa, Sabina Leanti; Kunath, Benoit J.; Robertson, Andrew; Pereira, Gabriel; Hagen, Live H.; Varghese, Neha J.; Qiu, Ling; Yao, Tianming; Flint, Gabrielle; Li, James; McDonald, Sean P.; Buttner, Duna; Pudlo, Nicholas A.; Schnizlein, Matthew K.; Young, Vincent B.; Brumer, Harry; Schmidt, Thomas M.; Terrapon, Nicolas; Lombard, Vincent; Henrissat, Bernard; Hamaker, Bruce; Eloe-Fadrosh, Emiley A.; Tripathi, Ashootosh; Pope, Phillip B.; Martens, Eric C. (April 2022). "Mechanistic insights into consumption of the food additive xanthan gum by the human gut microbiota". Nature Microbiology. 7 (4): 556–569. doi:10.1038/s41564-022-01093-0. hdl:11250/3003739. PMID 35365790. S2CID 247866305.
- ^ Hashimoto W, Nankai H, Mikami B, Murata K (2003). "Crystal structure of Bacillus sp. GL1 xanthan lyase, which acts on the side chains of xanthan". J. Biol. Chem. 278 (9): 7663–73. doi:10.1074/jbc.M208100200. PMID 12475987.
- Sutherland IW (1987). "Xanthan lyases--novel enzymes found in various bacterial species". J. Gen. Microbiol. 133 (11): 3129–34. doi:10.1099/00221287-133-11-3129. PMID 3446747.
