Glucono delta-lactone

Last updated
D-Gluconic acid δ-lactone [1] [2] [3]
Glucono-delta-lactone-2D-skeletal.svg
D-glucono-delta-lactone-3D-balls.png
Names
IUPAC name
D-Glucono-1,5-lactone
Systematic IUPAC name
(3R,4S,5S,6R)-3,4,5-Trihydroxy-6-(hydroxymethyl)oxan-2-one [2]
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.001.833 OOjs UI icon edit-ltr-progressive.svg
EC Number
  • 202-016-5
E number E575 (acidity regulators, ...)
KEGG
PubChem CID
UNII
  • InChI=1S/C6H10O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-5,7-10H,1H2/t2-,3-,4+,5-/m1/s1 Yes check.svgY
    Key: PHOQVHQSTUBQQK-SQOUGZDYSA-N Yes check.svgY
  • InChI=1/C6H10O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-5,7-10H,1H2/t2-,3-,4+,5-/m1/s1
    Key: PHOQVHQSTUBQQK-SQOUGZDYBO
  • C([C@@H]1[C@H]([C@@H]([C@H](C(=O)O1)O)O)O)O
Properties
C6H10O6
Molar mass 178.140 g·mol−1
Melting point 150–153 °C (302–307 °F; 423–426 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Glucono-delta-lactone (GDL), also known as gluconolactone, is an organic compound with the formula (HOCH)3(HOCH2CH)CO2. A colorless solid, it is an oxidized derivative of glucose.

Contents

It is typically produced by the aerobic oxidation of glucose in the presence of the enzyme glucose oxidase. The conversion cogenerates hydrogen peroxide, which is often the key product of the enzyme:

C6H12O6 + O2 → C6H10O6 + H2O2

Gluconolactone spontaneously hydrolyzes to gluconic acid: [4]

C6H10O6 + H2O → C6H12O7

Applications

Gluconolactone is a food additive with the E-number E575 [5] used as a sequestrant, an acidifier, [6] or a curing, pickling, or leavening agent. It is a lactone of D-gluconic acid. Pure GDL is a white odorless crystalline powder.

GDL has been marketed for use in feta cheese. [7] GDL is pH-neutral, but hydrolyses in water to gluconic acid which is acidic, adding a tangy taste to foods, though it has roughly a third of the sourness of citric acid. It is metabolized to 6-phospho-D-gluconate; one gram of GDL yields roughly the same amount of metabolic energy as one gram of sugar.

Upon addition to water, GDL is partially hydrolysed to gluconic acid, with the balance between the lactone form and the acid form established as a chemical equilibrium. The rate of hydrolysis of GDL is increased by heat and high pH. [8]

The yeast Saccharomyces bulderi can be used to ferment gluconolactone to ethanol and carbon dioxide. The pH value greatly affects culture growth. Gluconolactone at 1 or 2% in a mineral media solution causes the pH to drop below 3. [9]

It is also a complete inhibitor of the enzyme amygdalin beta-glucosidase at concentrations of 1 mM. [10]

See also

Related Research Articles

<span class="mw-page-title-main">Glucose</span> Naturally produced monosaccharide

Glucose is a sugar with the molecular formula C6H12O6. Glucose is overall the most abundant monosaccharide, a subcategory of carbohydrates. Glucose is mainly made by plants and most algae during photosynthesis from water and carbon dioxide, using energy from sunlight, where it is used to make cellulose in cell walls, the most abundant carbohydrate in the world.

Lactones are cyclic carboxylic esters are intramolecular esters derived from hydroxy carboxylic acids. They can be saturated or unsaturated. Some contain heteroatoms replacing one or more carbon atoms of the ring.

<span class="mw-page-title-main">Glucose oxidase</span> Class of enzymes

The glucose oxidase enzyme also known as notatin is an oxidoreductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.

<span class="mw-page-title-main">Gluconic acid</span> Chemical compound

Gluconic acid is an organic compound with molecular formula C6H12O7 and condensed structural formula HOCH2(CHOH)4CO2H. A white solid, it forms the gluconate anion in neutral aqueous solution. The salts of gluconic acid are known as "gluconates". Gluconic acid, gluconate salts, and gluconate esters occur widely in nature because such species arise from the oxidation of glucose. Some drugs are injected in the form of gluconates.

β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, acid invertase, and the systematic name: β-fructofuranosidase. The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertase is a glycoprotein that hydrolyses (cleaves) the non-reducing terminal β-fructofuranoside residues. Invertases cleave the O-C(fructose) bond, whereas the sucrases cleave the O-C(glucose) bond. Invertase cleaves the α-1,2-glycosidic bond of sucrose.

<span class="mw-page-title-main">Soured milk</span> Milk-based food product

Soured milk denotes a range of food products produced by the acidification of milk. Acidification, which gives the milk a tart taste, is achieved either through bacterial fermentation or through the addition of an acid, such as lemon juice or vinegar. The acid causes milk to coagulate and thicken, inhibiting the growth of harmful bacteria and improving the product's shelf life. It is not good for making cheese.

<small>L</small>-gulonolactone oxidase Enzyme involved in the synthesis of vitamin C

L-Gulonolactone oxidase is an enzyme that produces vitamin C, but is non-functional in Haplorrhini, in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action.

<span class="mw-page-title-main">Sodium erythorbate</span> Chemical compound

Sodium erythorbate (C6H7NaO6) is a food additive used predominantly in meats, poultry, and soft drinks. Chemically, it is the sodium salt of erythorbic acid. When used in processed meat such as hot dogs and beef sticks, it increases the rate at which nitrite reduces to nitric oxide, thus facilitating a faster cure and retaining the pink coloring. As an antioxidant structurally related to vitamin C, it helps improve flavor stability and prevents the formation of carcinogenic nitrosamines. When used as a food additive, its E number is E316. The use of erythorbic acid and sodium erythorbate as a food preservative has increased greatly since the U.S. Food and Drug Administration banned the use of sulfites as preservatives in foods intended to be eaten fresh (such as ingredients for fresh salads) and as food processors have responded to the fact that some people are allergic to sulfites. It can also be found in bologna, and is occasionally used in beverages, baked goods, and potato salad. Sodium erythorbate is produced from sugars derived from different sources, such as beets, sugarcane, and corn. Sodium erythorbate is usually produced via a fermentation process from D-glucose by Pseudomonas fluorescens bacteria. Most syntheses proceed through the 2-keto-D-gluconic acid intermediate. An urban myth claims that sodium erythorbate is made from ground earthworms; however, there is no truth to the myth. It is thought that the origin of the legend comes from the similarity of the chemical name to the words earthworm and bait.

<span class="mw-page-title-main">6-phosphogluconolactonase</span> Cytosolic enzyme

6-Phosphogluconolactonase (EC 3.1.1.31, 6PGL, PGLS, systematic name 6-phospho-D-glucono-1,5-lactone lactonohydrolase) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway:

<span class="mw-page-title-main">Glucose 1-dehydrogenase</span>

In enzymology, a glucose 1-dehydrogenase (EC 1.1.1.47) is an enzyme that catalyzes the chemical reaction

In enzymology, a glucose 1-dehydrogenase (NADP+) (EC 1.1.1.119) is an enzyme that catalyzes the chemical reaction

In enzymology, a L-galactonolactone oxidase (EC 1.3.3.12) is an enzyme that catalyzes the chemical reaction

In enzymology, a hexose oxidase (EC 1.1.3.5) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Pyranose oxidase</span>

In enzymology, a pyranose oxidase (EC 1.1.3.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a quinoprotein glucose dehydrogenase is an enzyme that catalyzes the chemical reaction

The enzyme amygdalin β-glucosidase (EC 3.2.1.117) catalyzes the following chemical reaction:

Selenium yeast is a feed additive for livestock, used to increase the selenium content in their fodder. It is a form of selenium currently approved for human consumption in the EU and Britain. Inorganic forms of selenium are used in feeds. Since these products can be patented, producers can demand premium prices. It is produced by fermenting Saccharomyces cerevisiae in a selenium-rich media.

<span class="mw-page-title-main">Triacetic acid lactone</span> Chemical compound

Triacetic acid lactone is an organic compound derived enzymatically from glucose. It is a light yellow solid that is soluble in organic solvents.

Aerobic fermentation or aerobic glycolysis is a metabolic process by which cells metabolize sugars via fermentation in the presence of oxygen and occurs through the repression of normal respiratory metabolism. Preference of aerobic fermentation over aerobic respiration is referred to as the Crabtree effect in yeast, and is part of the Warburg effect in tumor cells. While aerobic fermentation does not produce adenosine triphosphate (ATP) in high yield, it allows proliferating cells to convert nutrients such as glucose and glutamine more efficiently into biomass by avoiding unnecessary catabolic oxidation of such nutrients into carbon dioxide, preserving carbon-carbon bonds and promoting anabolism.

<span class="mw-page-title-main">Discovery and development of gastrointestinal lipase inhibitors</span>

Lipase inhibitors belong to a drug class that is used as an antiobesity agent. Their mode of action is to inhibit gastric and pancreatic lipases, enzymes that play an important role in the digestion of dietary fat. Lipase inhibitors are classified in the ATC-classification system as A08AB . Numerous compounds have been either isolated from nature, semi-synthesized, or fully synthesized and then screened for their lipase inhibitory activity but the only lipase inhibitor on the market is orlistat . Lipase inhibitors have also shown anticancer activity, by inhibiting fatty acid synthase.

References

  1. Budavari, Susan, ed. (2001), The Merck Index: An Encyclopedia of Chemicals, Drugs, and Biologicals (13th ed.), Merck, ISBN   0911910131 ,4469.
  2. 1 2 PubChem. "D-Gluconic acid, delta-lactone". pubchem.ncbi.nlm.nih.gov. Archived from the original on 2022-02-25. Retrieved 2022-05-03.
  3. Beil. 18, V, 5, 11
  4. Wong, Chun Ming; Wong, Kwun Hei; Chen, Xiao Dong (2008). "Glucose oxidase: Natural Occurrence, Function, Properties and Industrial Applications". Applied Microbiology and Biotechnology. 78 (6): 927–938. doi:10.1007/s00253-008-1407-4. PMID   18330562. S2CID   2246466.
  5. "Current EU approved additives and their E Numbers". Food Standards Agency. Archived from the original on 22 April 2022.
  6. Martin, F.; Cayot, N.; Marin, A.; et al. (2009). "Effect of oxidoreduction potential and of gas bubbling on rheological properties and microstructure of acid skim milk gels acidified with glucono-δ-lactone" (PDF). Journal of Dairy Science. 92 (12): 5898–5906. doi: 10.3168/jds.2009-2491 . PMID   19923593. Archived (PDF) from the original on 2020-03-11. Retrieved 2019-08-16.
  7. Blythman, Joanna (21 February 2015). "Inside the food industry: the surprising truth about what you eat". The Guardian. Archived from the original on 13 August 2016. Retrieved 28 October 2016.{{cite web}}: CS1 maint: bot: original URL status unknown (link)
  8. Pocker, Y.; Green, Edmond (1973). "Hydrolysis of D-Glucono-δ-lactone. I. General Acid–Base Catalysis, Solvent Deuterium Isotope Effects, and Transition State Characterization". J. Am. Chem. Soc. 95 (1): 113–19. doi:10.1021/ja00782a019. PMID   4682891.
  9. Van Dijken, J. P.; Van Tuijl, A.; Luttik, M. A.; Middelhoven, W. J.; Pronk, J. T. (2002). "Novel pathway for alcoholic fermentation of delta-gluconolactone in the yeast Saccharomyces bulderi". Journal of Bacteriology. 184 (3): 672–678. doi:10.1128/JB.184.3.672-678.2002. PMC   139522 . PMID   11790736.
  10. Petruccioli, M.; Brimer, L.; Cicalini, A. R.; Federici, F. (1999). "Production and Properties of the Linamarase and Amygdalase Activities of Penicillium aurantiogriseum P35". Bioscience, Biotechnology, and Biochemistry. 63 (5): 805–812. doi: 10.1271/bbb.63.805 . PMID   10380623.