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Trehalose

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Not to be confused with Trehalulose.
Trehalose
Names
IUPAC name
α-D-glucopyranosyl-(1→1)-α-D-glucopyranoside
Systematic IUPAC name
(2R,3S,4S,5R,6R)-2-(Hydroxymethyl)-6-[(2R,3R,4S,5S,6R)-3,4, 5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxane-3,4,5-triol
Other names
α,α‐Trehalose
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.002.490 Edit this at Wikidata
UNII
  • InChI=1S/C12H22O11/c13-1-3-5(15)7(17)9(19)11(21-3)23-12-10(20)8(18)6(16)4(2-14)22-12/h3-20H,1-2H2/t3-,4-,5-,6-,7+,8+,9-,10-,11-,12-/m1/s1 checkY
    Key: HDTRYLNUVZCQOY-LIZSDCNHSA-N checkY
  • InChI=1/C12H22O11/c13-1-3-5(15)7(17)9(19)11(21-3)23-12-10(20)8(18)6(16)4(2-14)22-12/h3-20H,1-2H2/t3-,4-,5-,6-,7+,8+,9-,10-,11-,12-/m1/s1
    Key: HDTRYLNUVZCQOY-LIZSDCNHBN
  • OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@H](O1)O[C@@H]2[C@H](O)[C@@H](O)[C@H](O)[C@H](O2)CO
Properties
C12H22O11 (anhydride)
Molar mass 342.296 g/mol (anhydrous)
378.33 g/mol (dihydrate)
Appearance White orthorhombic crystals
Density 1.58 g/cm3 at 24 °C
Melting point 203 °C (397 °F; 476 K) (anhydrous)
97 °C (dihydrate)
68.9 g per 100 g at 20 °C[1]
Solubility Slightly soluble in ethanol, insoluble in diethyl ether and benzene[2]
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)

Trehalose (from Turkish tıgala – a sugar derived from insect cocoons + -ose)[3] is a sugar consisting of two molecules of glucose. It is also known as mycose or tremalose. Some bacteria, fungi, plants and invertebrate animals synthesize it as a source of energy, and to survive freezing and lack of water.

Extracting trehalose was once a difficult and costly process, but around 2000, the Hayashibara company (Okayama, Japan) discovered an inexpensive extraction technology from starch.[4][5] Trehalose has high water retention capabilities, and is used in food, cosmetics and as a drug. A procedure developed in 2017 using trehalose allows sperm storage at room temperatures.[6]

Structure

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Trehalose is a disaccharide formed by a 1,1-glycosidic bond between two α-glucose units. It is found in nature as a disaccharide and also as a monomer in some polymers.[7] Two other stereoisomers exist: α,β-trehalose, also called neotrehalose, and β,β-trehalose, also called isotrehalose. Neither of these alternate isomers has been isolated from living organisms, but isotrehalose has been was found in starch hydroisolates.[7]

Synthesis

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At least three biological pathways support trehalose biosynthesis.[7] An industrial process can derive trehalose from corn starch.[8]

Properties

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Chemical

[edit]

Trehalose is a nonreducing sugar formed from two glucose units joined by a 1–1 alpha bond, giving it the name α-D-gluco­pyranosyl-(1→1)-α-D-gluco­pyranoside. The bonding makes trehalose very resistant to acid hydrolysis, and therefore is stable in solution at high temperatures, even under acidic conditions. The bonding keeps nonreducing sugars in closed-ring form, such that the aldehyde or ketone end groups do not bind to the lysine or arginine residues of proteins (a process called glycation). Trehalose is less soluble than sucrose, except at high temperatures (>80 °C). Trehalose forms a rhomboid crystal as the dihydrate, and has 90% of the calorific content of sucrose in that form. Anhydrous forms of trehalose readily regain moisture to form the dihydrate. Anhydrous forms of trehalose can show interesting physical properties when heat-treated.

Trehalose aqueous solutions show a concentration-dependent clustering tendency. Owing to their ability to form hydrogen bonds, they self-associate in water to form clusters of various sizes. All-atom molecular dynamics simulations showed that concentrations of 1.5–2.2 molar allow trehalose molecular clusters to percolate and form large and continuous aggregates.[9]

Trehalose directly interacts with nucleic acids, facilitates melting of double stranded DNA and stabilizes single-stranded nucleic acids.[10]

Biological

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Organisms ranging from bacteria, yeast, fungi, insects, invertebrates, and lower and higher plants have enzymes that can make trehalose.[7] In nature, trehalose can be found in plants, and microorganisms. In animals, trehalose is prevalent in shrimp, and also in insects, including grasshoppers, locusts, butterflies, and bees, in which trehalose serves as blood-sugar.[citation needed] Trehalase genes are found in tardigrades, the microscopic ecdysozoans found worldwide in diverse extreme environments.[11]

Trehalose is the major carbohydrate energy storage molecule used by insects for flight.[citation needed] One possible reason for this is that the glycosidic linkage of trehalose, when acted upon by an insect trehalase, releases two molecules of glucose, which is required for the rapid energy requirements of flight. This is double the efficiency of glucose release from the storage polymer starch, for which cleavage of one glycosidic linkage releases only one glucose molecule.[citation needed]

In plants, trehalose is seen in sunflower seeds, moonwort, Selaginella plants,[12] and sea algae. Within the fungi, it is prevalent in some mushrooms, such as shiitake (Lentinula edodes), oyster, king oyster, and golden needle.[13]

Even within the plant kingdom, Selaginella (sometimes called the resurrection plant), which grows in desert and mountainous areas, may be cracked and dried out, but will turn green again and revive after rain because of the function of trehalose.[12]

The two prevalent theories as to how trehalose works within the organism in the state of cryptobiosis are the vitrification theory, a state that prevents ice formation, or the water displacement theory, whereby water is replaced by trehalose.[11][14]

In bacterial cell wall, trehalose has a structural role in adaptive responses to stress such as osmotic differences and extreme temperature.[15] Yeast uses trehalose as a carbon source in response to abiotic stresses.[16] In humans, the only known function of trehalose is as a neuroprotective, which it accomplishes by inducing autophagy and thereby clearing protein aggregates.[citation needed]

Trehalose has also been reported for anti-bacterial, anti-biofilm, and anti-inflammatory (in vitro and in vivo) activities, upon its esterification with fatty acids of varying chain lengths.[17]

Nutritional and dietary properties

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Trehalose is rapidly broken down into glucose by the enzyme trehalase, which is present in the brush border of the intestinal mucosa of omnivores (including humans) and herbivores.[18]: 135  It causes less of a spike in blood sugar than glucose.[19] Trehalose has about 45% the sweetness of sucrose at concentrations above 22%, but when the concentration is reduced, its sweetness decreases more quickly than that of sucrose, so that a 2.3% solution tastes 6.5 times less sweet as the equivalent sugar solution.[20]: 444 

It is commonly used in prepared frozen foods, like ice cream, because it lowers the freezing point of foods.[19]

Deficiency of trehalase enzyme is unusual in humans, except in the Greenlandic Inuit, where it is present in only 10–15% of the population.[21]: 197 

Metabolism

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Five biosynthesis pathways have been reported for trehalose. The most common pathway is TPS/TPP pathway which is used by organisms that synthesize trehalose using the enzyme trehalose-6-phosphate (T6P) synthase (TPS).[22] Second, trehalose synthase (TS) in certain types of bacteria could produce trehalose by using maltose and another disaccharide with two glucose units as substrates.[23] Third, the TreY-TreZ pathway in some bacteria converts starch that contain maltooligosaccharide or glycogen directly into trehalose.[24] Fourth, in primitive bacteria, trehalose glycisyltransferring synthase (TreT) produces trehalose from ADP-glucose and glucose.[25] Fifth, trehalose phosphorylase (TreP) either hydrolyses trehalose into glucose-1-phosphate and glucose or may act reversibly in certain species.[26] Vertebrates do not have the ability to synthesize or store trehalose.[27] Trehalase in humans is found only in specific location such as the intestinal mucosa, renal brush-border, liver and blood. Expression of this enzyme in vertebrates is initially found during the gestation period that is the highest after weaning. Then, the level of trehalase remained constant in the intestine throughout life.[28] Meanwhile, diets consisting of plants and fungi contain trehalose. Moderate amount of trehalose in diet is essential and having low amount of trehalose could result in diarrhea, or other intestinal symptoms.[29]

Medical use

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Trehalose is an ingredient, along with hyaluronic acid, in an artificial tears product used to treat dry eye.[30][16] Outbreaks of Clostridioides difficile were initially associated with trehalose,[19][31][32] but this finding was disputed in 2019.[33]

In 2021, the FDA accepted an Investigational New Drug (IND) application and granted fast track status for an injectable form of trehalose (SLS-005) as a potential treatment for spinocerebellar ataxia type 3 (SCA3).[34][35]

History

[edit]

In 1832, H.A.L. Wiggers discovered trehalose in an ergot of rye,[36] and in 1859 Marcellin Berthelot isolated it from Trehala manna, a substance made by weevils and named it trehalose.[37]

Trehalose has long been known as an autophagy inducer that acts independently of mTOR.[38] In 2017, research was published showing that trehalose induces autophagy by activating TFEB,[39] a protein that acts as a master regulator of the autophagy-lysosome pathway.[40]

See also

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References

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  1. ^ Higashiyama T (2002). "Novel functions and applications of trehalose" (PDF). Pure Appl. Chem. 74 (7): 1263–1269. doi:10.1351/pac200274071263. S2CID 28311022.
  2. ^ Lide, David R. (1998). Handbook of Chemistry and Physics (87 ed.). Boca Raton, Florida: CRC Press. pp. 3–534. ISBN 978-0-8493-0594-8.
  3. ^ "Trehalose | Definition of Trehalose by Lexico". Archived from the original on February 26, 2022.
  4. ^ Cargill, Incorporated (30 May 2011). "Cargill, Hayashibara to Introduce Trehalose Sweetener to the Americas". PR Newswire. Retrieved 2011-07-31.
  5. ^ "JAPAN: Cargill, Hayashibara to Introduce Trehalose Sweetener to the Americas". just-food.com. 2000-05-31. Retrieved 2 February 2013.
  6. ^ Patrick, Jennifer L.; Elliott, Gloria D.; Comizzoli, Pierre (1 November 2017). "Structural integrity and developmental potential of spermatozoa following microwave-assisted drying in the domestic cat model". Theriogenology. 103: 36–43. doi:10.1016/j.theriogenology.2017.07.037. PMID 28772113.
  7. ^ a b c d Elbein AD, Pan YT, Pastuszak I, Carroll D (April 2003). "New insights on trehalose: a multifunctional molecule". Glycobiology. 13 (4): 17R–27R. doi:10.1093/glycob/cwg047. PMID 12626396.
  8. ^ [dead link]"GRAS Notification for Hayashibara Trehalose" (PDF). Food and Drug Administration. May 3, 2000: 10. {{cite journal}}: Cite journal requires |journal= (help)
  9. ^ Sapir L, Harries D (February 2011). "Linking trehalose self-association with binary aqueous solution equation of state". The Journal of Physical Chemistry B. 115 (4): 624–34. doi:10.1021/jp109780n. PMID 21186829.
  10. ^ Bezrukavnikov S, Mashaghi A, van Wijk RJ, Gu C, Yang LJ, Gao YQ, Tans SJ (October 2014). "Trehalose facilitates DNA melting: a single-molecule optical tweezers study". Soft Matter. 10 (37): 7269–77. Bibcode:2014SMat...10.7269B. doi:10.1039/C4SM01532K. PMID 25096217.
  11. ^ a b Kamilari, Maria; Jørgensen, Aslak; Schiøtt, Morten; Møbjerg, Nadja (2019-07-24). "Comparative transcriptomics suggest unique molecular adaptations within tardigrade lineages". BMC Genomics. 20 (1): 607. doi:10.1186/s12864-019-5912-x. ISSN 1471-2164. PMC 6652013. PMID 31340759.
  12. ^ a b Zentella R, Mascorro-Gallardo JO, Van Dijck P, Folch-Mallol J, Bonini B, Van Vaeck C, Gaxiola R, Covarrubias AA, Nieto-Sotelo J, Thevelein JM, Iturriaga G (April 1999). "A Selaginella lepidophylla trehalose-6-phosphate synthase complements growth and stress-tolerance defects in a yeast tps1 mutant". Plant Physiology. 119 (4): 1473–82. doi:10.1104/pp.119.4.1473. PMC 32033. PMID 10198107.
  13. ^ Reis FS, Barros L, Martins A, Ferreira IC (February 2012). "Chemical composition and nutritional value of the most widely appreciated cultivated mushrooms: an inter-species comparative study" (PDF). Food and Chemical Toxicology. 50 (2): 191–7. doi:10.1016/j.fct.2011.10.056. hdl:10198/7341. PMID 22056333. S2CID 23997767.
  14. ^ Sola-Penna M, Meyer-Fernandes JR (December 1998). "Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: why is trehalose more effective than other sugars?". Archives of Biochemistry and Biophysics. 360 (1): 10–4. doi:10.1006/abbi.1998.0906. PMID 9826423.
  15. ^ Iturriaga, Gabriel; Suárez, Ramón; Nova-Franco, Barbara (2009). "Trehalose Metabolism: From Osmoprotection to Signaling". International Journal of Molecular Sciences. 10 (9): 3793–3810. doi:10.3390/ijms10093793. PMC 2769160. PMID 19865519.
  16. ^ a b Pucker AD, Ng SM, Nichols JJ (February 2016). "Over the counter (OTC) artificial tear drops for dry eye syndrome". The Cochrane Database of Systematic Reviews. 2016 (2): CD009729. doi:10.1002/14651858.CD009729.pub2. PMC 5045033. PMID 26905373.
  17. ^ Marathe, Sandesh J.; Shah, Nirali N.; Singhal, Rekha S. (2020-01-01). "Enzymatic synthesis of fatty acid esters of trehalose: Process optimization, characterization of the esters and evaluation of their bioactivities". Bioorganic Chemistry. 94: 103460. doi:10.1016/j.bioorg.2019.103460. ISSN 0045-2068. PMID 31791682. S2CID 208610507.
  18. ^ Mathlouthi, M., ed. (1999). Food packaging and preservation. Gaithersburg, Md.: Aspen Publishers. ISBN 978-0-8342-1349-4. Retrieved 25 June 2014.
  19. ^ a b c Collins F (9 January 2018). "Has an Alternative to Table Sugar Contributed to the C. Diff. Epidemic?". NIH Director's Blog.
  20. ^ O'Brien-Nabors, Lyn, ed. (2012). Alternative sweeteners (4th ed.). Boca Raton: CRC Press. ISBN 978-1-4398-4614-8. Retrieved 25 June 2014.
  21. ^ Kohlmeier M (2003). Nutrient Metabolism. Burlington: Elsevier. ISBN 978-0-08-053789-4. Retrieved 25 June 2014.
  22. ^ Cabib, E.; Leloir, L. F. (1958). "The biosynthesis of trehalose phosphate". The Journal of Biological Chemistry. 231 (1): 259–275. doi:10.1016/S0021-9258(19)77303-7. hdl:11336/135983. ISSN 0021-9258. PMID 13538966.
  23. ^ Nishimoto, T.; Nakano, M.; Nakada, T.; Chaen, H.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y. (April 1996). "Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48". Bioscience, Biotechnology, and Biochemistry. 60 (4): 640–644. doi:10.1271/bbb.60.640. ISSN 0916-8451. PMID 8829531.
  24. ^ Maruta, Kazuhiko; Mitsuzumi, Hitoshi; Nakada, Tetsuya; Kubota, Michio; Chaen, Hiroto; Fukuda, Shigeharu; Sugimoto, Toshiyuki; Kurimoto, Masashi (1996-12-06). "Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius". Biochimica et Biophysica Acta (BBA) - General Subjects. 1291 (3): 177–181. doi:10.1016/S0304-4165(96)00082-7. ISSN 0304-4165. PMID 8980629.
  25. ^ Qu, Qiuhao; Lee, Sung-Jae; Boos, Winfried (2004-11-12). "TreT, a Novel Trehalose Glycosyltransferring Synthase of the Hyperthermophilic Archaeon Thermococcus litoralis*". Journal of Biological Chemistry. 279 (46): 47890–47897. doi:10.1074/jbc.M404955200. ISSN 0021-9258. PMID 15364950.
  26. ^ Ren, Yuanyuan; Dai, Xiuyu; Zhou, Jian; Liu, Jingfang; Pei, Huadong; Xiang, Hua (2005-05-01). "Gene expression and molecular characterization of a thermostable trehalose phosphorylase fromThermoanaerobacter tengcongensis". Science in China Series C: Life Sciences. 48 (3): 221–227. doi:10.1007/BF03183615. ISSN 1862-2798. PMID 16092754. S2CID 23443429.
  27. ^ Elbein, Alan D. (1974-01-01), Tipson, R. Stuart; Horton, Derek (eds.), "The Metabolism of α,α-Trehalose**The work cited from the author's laboratory was supported by grants from the Robert A. Welch Foundation and the National Institutes of Health (AI 09402).", Advances in Carbohydrate Chemistry and Biochemistry, 30, Academic Press: 227–256, doi:10.1016/S0065-2318(08)60266-8, PMID 4377836, retrieved 2021-11-30
  28. ^ Galand, G. (1989). "Brush border membrane sucrase-isomaltase, maltase-glucoamylase and trehalase in mammals. Comparative development, effects of glucocorticoids, molecular mechanisms, and phylogenetic implications". Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 94 (1): 1–11. doi:10.1016/0305-0491(89)90002-3. ISSN 0305-0491. PMID 2513162.
  29. ^ Thevelein, J M (March 1984). "Regulation of trehalose mobilization in fungi". Microbiological Reviews. 48 (1): 42–59. doi:10.1128/mr.48.1.42-59.1984. ISSN 0146-0749. PMC 373002. PMID 6325857.
  30. ^ Pinto-Bonilla JC, Del Olmo-Jimeno A, Llovet-Osuna F, Hernández-Galilea E (2015). "A randomized crossover study comparing trehalose/hyaluronate eyedrops and standard treatment: patient satisfaction in the treatment of dry eye syndrome". Therapeutics and Clinical Risk Management. 11: 595–603. doi:10.2147/TCRM.S77091. PMC 4403513. PMID 25926736.
  31. ^ Ballard JD (January 2018). "Pathogens boosted by food additive". Nature. 553 (7688): 285–286. doi:10.1038/d41586-017-08775-4. PMID 29345660.
  32. ^ Collins J, Robinson C, Danhof H, Knetsch CW, van Leeuwen HC, Lawley TD, Auchtung JM, Britton RA (January 2018). "Dietary trehalose enhances virulence of epidemic Clostridium difficile". Nature. 553 (7688): 291–294. Bibcode:2018Natur.553..291C. doi:10.1038/nature25178. PMC 5984069. PMID 29310122.
  33. ^ Eyre, David W.; Didelot, Xavier; Buckley, Anthony M.; Freeman, Jane; Moura, Ines B.; Crook, Derrick W.; Peto, Tim E.A.; Walker, A. Sarah; Wilcox, Mark H.; Dingle, Kate E. (2019). "Clostridium difficile trehalose metabolism variants are common and not associated with adverse patient outcomes when variably present in the same lineage". eBioMedicine. 43: 347–355. doi:10.1016/j.ebiom.2019.04.038. ISSN 2352-3964. PMC 6558026. PMID 31036529.
  34. ^ Park, Brian (8 November 2021). "Trehalose Fast Tracked for Spinocerebellar Ataxia". MPR. Retrieved 14 November 2023.
  35. ^ "FDA Accepts Investigational New Drug Application and Grants Fast Track Designation of Trehalose for Spinocerebellar Ataxia Treatment". Practical Neurology. 12 November 2021. Retrieved 14 November 2023.
  36. ^ Wiggers HA (1832). "Untersuchung über das Mutterkorn, Secale cornutum". Annalen der Pharmacie. 1 (2): 129–182. doi:10.1002/jlac.18320010202.
  37. ^ Tillequin F (July 2009). "Le Tréhala, une drogue à la croisée des chemins" [Trehala, a meeting point between zoology, botany, chemistry, and biochemistry]. Revue d'Histoire de la Pharmacie (in French). 57 (362): 163–72. doi:10.3406/pharm.2009.22043. PMID 20027793.
  38. ^ Menzies FM, Fleming A, Rubinsztein DC (June 2015). "Compromised autophagy and neurodegenerative diseases". Nature Reviews. Neuroscience. 16 (6): 345–57. doi:10.1038/nrn3961. PMID 25991442. S2CID 19272817.
  39. ^ Sharma J, di Ronza A, Lotfi P, Sardiello M (July 2018). "Lysosomes and Brain Health". Annual Review of Neuroscience. 41: 255–276. doi:10.1146/annurev-neuro-080317-061804. PMID 29661037. S2CID 207581692.
  40. ^ Sardiello M (May 2016). "Transcription factor EB: from master coordinator of lysosomal pathways to candidate therapeutic target in degenerative storage diseases". Annals of the New York Academy of Sciences. 1371 (1): 3–14. Bibcode:2016NYASA1371....3S. doi:10.1111/nyas.13131. PMC 5032832. PMID 27299292.
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