User:Traversoe/sandbox
| Glucanase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3D crystalline structure of the endoglucanase Cel10 from Klebsiella pneumoniae. | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.1. | ||||||||
| CAS no. | 9015-78-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Glucanase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | Eng1p | ||||||
| CAS number | |||||||
| PDB | 5GY3 | ||||||
| RefSeq | WP_012967086.1 | ||||||
| UniProt | A0A0J4VP90 | ||||||
| |||||||
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds.[1] Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat.[1] Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases.[1] Many types of glucanases share similar amino acid sequences but vastly different substrates.[1] Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.[1]
Structure[edit]
α-glucanases[edit]
- some common alpha-gases
β-glucanases[edit]
The secondary and tertiary structures of β-glucanases involves the stacking of multiple β-sheets, each of which are made of several anti-parallel strands that bend and form a cleft crossing the active site of the enzyme.[1] This type of structure has been called the "jelly roll fold."
Some common β-glucanases[edit]
- 1,3-β-glucanases (laminarinases, EC 3.2.1.39)[1]
The functional formation of the enzyme-substrate complex is dictated by the induced-fit mechanism.
Mechanism of Enzyme Action[edit]
The main function of glucanase is to catalyze the hydrolysis of glycosidic bonds in polysaccharides. This function is not highly specific, and the enzymes distinguish among substrates mostly by the types of bonds present and α- or β- configuration.[2]
In 1953, Dr. D. E. Koshland proposed a double-displacement mechanism for this enzyme action.[3] The first step of his proposed mechanism is rate-limiting step independent of the concentration of the substrate and involves an amino acid nucleophile and an acid/base catalyst.[3] In this step, the nucleophile, with help from the acid residue, displaces the aglycone and forms a covalent glycosyl-enzyme intermediate.[3][1] The second step involves a water molecule, assisted by the conjugate base of the acid catalyst, rendering the free sugar while retaining an anomeric configuration of the molecule.[1]
Glucanases can also catalyze transglycosylation, resulting in new β-glycosidic bonds between donor and acceptor saccharides.[1] This reaction, which has the same region- and stereo-specificity as the hydrolysis reaction, involves either the direct reversal of hydrolysis (known as condensation) or kinetic control of a glycosyl donor substrate.[1]
Microbial Occurrence and Agricultural Significance[edit]
Microbial Production[edit]
Bacteria such as E. coli, and Bacillus spp. produce 1,3-1,4-β-glucanases in order to degrade and use polysaccharides from their environment as an energy source.[1] These bacterial glucanases are an example of convergent evolution as they share similarity or relation with plant glucanase primary, secondary, or tertiary structure.[1] Glucanases have also been found to be secreted by fungi such as Saccharomyces cerevisiae and the anaerobic fungus Orpinomyces.[1][4]
Beer and Wine[edit]
When bacterial 1,3-1,4-β-glucanases are heat inactivated, causing the build-up of high molecular-weight glucans which can result in reduced extract yield, lower filtration rates, and even gelatinous precipitates in the finished product.[1]
Used in enological practices during the aging process of wine, particularly when aged on lees with microxygenation. The enzyme aids in autolysis of yeast cells to release polysaccharides and mannoproteins, which is believed to aid in the color and texture of the wine.
Livestock Feed[edit]
In the production of feedstuff for broiler chickens and piglets, it has been found that β-glucanases improve digestibility of barley-based diets.[1]
References[edit]
- ^ a b c d e f g h i j k l m n o p Planas, Antoni (2000-12-29). "Bacterial 1,3-1,4-β-glucanases: structure, function and protein engineering". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. Protein engineering of enzymes. 1543 (2): 361–382. doi:10.1016/S0167-4838(00)00231-4. ISSN 0167-4838.
- ^ "DMS35_22185 - Glucanase - Klebsiella variicola - DMS35_22185 gene & protein". www.uniprot.org. Retrieved 2021-11-02.
- ^ a b c Koshland, D. E. (1953). "Stereochemistry and the Mechanism of Enzymatic Reactions". Biological Reviews. 28 (4): 416–436. doi:10.1111/j.1469-185X.1953.tb01386.x. ISSN 1469-185X.
- ^ Baladrón, Victoriano; Ufano, Sandra; Dueñas, Encarnación; Martín-Cuadrado, Ana Belén; del Rey, Francisco; Vázquez de Aldana, Carlos R. (2002-10-01). "Eng1p, an Endo-1,3-β-Glucanase Localized at the Daughter Side of the Septum, Is Involved in Cell Separation in Saccharomyces cerevisiae". Eukaryotic Cell. 1 (5): 774–786. doi:10.1128/EC.1.5.774-786.2002. PMC 126745. PMID 12455695.
{{cite journal}}: CS1 maint: PMC format (link)
Further reading[edit]
- Attigani A, Sun L, Wang Q, Liu Y, Bai D, Li S, Huang X (December 2016). "The crystal structure of the endoglucanase Cel10, a family 8 glycosyl hydrolase from Klebsiella pneumoniae". Acta Crystallographica. Section F, Structural Biology Communications. 72 (Pt 12): 870–876. doi:10.1107/S2053230X16017891. PMC 5137463. PMID 27917834.
- Bernardi AV, de Gouvêa PF, Gerolamo LE, Yonamine DK, de Lourdes de Lima Balico L, Uyemura SA, Dinamarco TM (October 2018). "Functional characterization of GH7 endo-1,4-β-glucanase from Aspergillus fumigatus and its potential industrial application". Protein Expression and Purification. 150: 1–11. doi:10.1016/j.pep.2018.04.016. PMID 29715559. S2CID 19171160.
- Ariaeenejad S, Sheykh Abdollahzadeh Mamaghani A, Maleki M, Kavousi K, Foroozandeh Shahraki M, Hosseini Salekdeh G (October 2020). "A novel high performance in-silico screened metagenome-derived alkali-thermostable endo-β-1,4-glucanase for lignocellulosic biomass hydrolysis in the harsh conditions". BMC Biotechnology. 20 (1): 56. doi:10.1186/s12896-020-00647-6. PMC 7574624. PMID 33076889.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Li J, Cao C, Jiang Y, Huang Q, Shen Y, Ni J (December 2020). "A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi". Applied Biochemistry and Biotechnology. 192 (4): 1284–1297. doi:10.1007/s12010-020-03368-w. PMID 32725373. S2CID 220808988.
- Furtado GP, Carli S, Meleiro LP, Salgado JC, Ward RJ (December 2021). "Enhanced hydrolytic efficiency of an engineered CBM11-glucanase enzyme chimera against barley β-d-glucan extracts". Food Chemistry. 365: 130460. doi:10.1016/j.foodchem.2021.130460. PMID 34237573.
- Villettaz JC, Steiner D, Trogus H (January 1984). "The use of a beta glucanase as an enzyme in wine clarification and filtration". American Journal of Enology and Viticulture. 35 (4): 253–6.
- Mathlouthi N, Mallet S, Saulnier L, Quemener B, Larbier M (September 2002). "Effects of xylanase and β-glucanase addition on performance, nutrient digestibility, and physico-chemical conditions in the small intestine contents and caecal microflora of broiler chickens fed a wheat and barley-based diet". Animal Research. 51 (5): 395–406. doi:10.1051/animres:2002034.
- Maclachlan G, Brady C (July 1994). "Endo-1,4-[beta]-Glucanase, Xyloglucanase, and Xyloglucan Endo-Transglycosylase Activities Versus Potential Substrates in Ripening Tomatoes". Plant Physiology. 105 (3): 965–974. doi:10.1104/pp.105.3.965. PMC 160747. PMID 12232258.
- Salyers AA, Palmer JK, Wilkins TD (May 1977). "Laminarinase (beta-glucanase) activity in Bacteroides from the human colon". Applied and Environmental Microbiology. 33 (5): 1118–1124. Bibcode:1977ApEnM..33.1118S. doi:10.1128/aem.33.5.1118-1124.1977. PMC 170836. PMID 879772.
- Marco JL, Felix CR (2007). "Purification and characterization of a beta-Glucanase produced by Trichoderma harzianum showing biocontrol potential". Brazilian Archives of Biology and Technology. 50: 21–9. doi:10.1590/S1516-89132007000100003.
- Keitel T, Simon O, Borriss R, Heinemann U (June 1993). "Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase". Proceedings of the National Academy of Sciences of the United States of America. 90 (11): 5287–5291. Bibcode:1993PNAS...90.5287K. doi:10.1073/pnas.90.11.5287. PMC 46701. PMID 8099449.
- Teather RM, Erfle JD (July 1990). "DNA sequence of a Fibrobacter succinogenes mixed-linkage beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase) gene". Journal of Bacteriology. 172 (7): 3837–3841. doi:10.1128/jb.172.7.3837-3841.1990. PMC 213364. PMID 2193918.
- Yang P, Shi P, Wang Y, Bai Y, Meng K, Luo H, et al. (January 2007). "Cloning and overexpression of a Paenibacillus beta-glucanase in Pichia pastoris: purification and characterization of the recombinant enzyme". Journal of Microbiology and Biotechnology. 17 (1): 58–66. PMID 18051354.
- Esteve-Garcia E, Brufau J, Pérez-Vendrell A, Miquel A, Duven K (December 1997). "Bioefficacy of enzyme preparations containing beta-glucanase and xylanase activities in broiler diets based on barley or wheat, in combination with flavomycin". Poultry Science. 76 (12): 1728–1737. doi:10.1093/ps/76.12.1728. PMID 9438289.
- Ebisu S, Kato K, Kotani S, Misaki A (December 1975). "Isolation and purification of Flavobacterium alpha-1,3-glucanase-hydrolyzing, insoluble, sticky glucan of Streptococcus mutans". Journal of Bacteriology. 124 (3): 1489–1501. doi:10.1128/jb.124.3.1489-1501.1975. PMC 236064. PMID 370.
- Takehara T, Inoue M, Morioka T, Yokogawa K (February 1981). "Purification and properties of endo-alpha-1,3-glucanase from a Streptomyces chartreusis strain". Journal of Bacteriology. 145 (2): 729–735. doi:10.1128/jb.145.2.729-735.1981. PMC 217172. PMID 7462159.
- Inoue M, Yakushiji T, Mizuno J, Yamamoto Y, Tanii S (December 1990). "Inhibition of dental plaque formation by mouthwash containing an endo-alpha-1, 3 glucanase". Clinical Preventive Dentistry. 12 (5): 10–14. PMID 2095311.
- McCleary BV (November 1980). "New chromogenic substrates for the assay of alpha-amylase and (1→4)-beta-D-glucanase". Carbohydrate Research. 86 (1): 97–104. doi:10.1016/s0008-6215(00)84584-x. PMID 6159974.