Xanthan lyase

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xanthan lyase
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EC no. 4.2.2.12
CAS no. 113573-69-6
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The enzyme xanthan lyase (EC 4.2.2.12) catalyzes the following process:

Contents

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.

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References

  1. 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.
  2. 1 2 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. doi:10.1128/AEM.64.10.3765-3768.1998. PMC   106543 . PMID   9758797.
  3. 1 2 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. doi:10.1128/AEM.65.6.2446-2452.1999. PMC   91360 . PMID   10347025.
  4. 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. PMID   35365790. S2CID   247866305.
  5. 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.