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Riboflavin a water-soluble B fraction was found in the 1920s to contain a yellow, fluorescent growth factor called riboflavin in England and vitamin G in the United States.
Riboflavin is prescribed to treat corneal thinning, and taken orally, may reduce the incidence of migraine headaches in adults.
Riboflavin deficiency is rare and is usually accompanied by deficiencies of other vitamins and nutrients.
CAS Number: 83-88-5
Molecular Formula: C17H20N4O6
Molecular Weight: 376.36
EINECS Number: 201-507-1
Synonyms: riboflavin, vitamin B2, 83-88-5, Riboflavine, Riboflavin, Vitamin G, (-)-riboflavin, Riboflavine, Flavaxin, Riboflavinum, Beflavin, Beflavine, Riboflavina, Lactobene, Ribocrisina, Riboderm, Ribotone, Vitaflavine, Flaxain, Ribipca, Ribosyn, Ribovel, Vitamin Bi, Flavin BB, Russupteridine Yellow III, Vitasan B2, HYRE, Bisulase, Riboflavinequinone, 7,8-Dimethyl-10-ribitylisoalloxazine, 6,7-Dimethyl-9-D-ribitylisoalloxazine, Lacto-flavin, Fiboflavin, Dermadram, E101, vitamin-b2, HSDB 817, Aqua-Flave, C.I. Food Yellow 15, Riboflavin (Vit B2), CCRIS 1904, Ins no.101(iii), CHEBI:17015, Ins-101(iii), Riboflavin (Vitamin B2), UNII-TLM2976OFR, 7,8-Dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)isoalloxazine, EINECS 201-507-1, E-101(iii), TLM2976OFR, Vitamin b2 (as riboflavin), MFCD00005022, NSC 33298, Vitamin B-2, 7,8-dimethyl-10-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]benzo[g]pteridine-2,4-dione, DTXSID8021777, AI3-14697, INS NO. 101(I), Isoalloxazine, 7,8-dimethyl-10-D-ribityl-, C.I. 50900, NSC-33298, NCI-0033298, 1-Deoxy-1-(3,4-dihydro-7,8-dimethyl-2,4-dioxobenzo[g]pteridin-10(2H)-yl)-D-ribitol, 7,8-dimethyl-10-((2S,3S,4R)-2,3,4,5-tetrahydroxypentyl)benzo[g]pteridine-2,4(3H,10H)-dione, D-Ribitol, 1-deoxy-1-(3,4-dihydro-7,8-dimethyl-2,4-dioxobenzo(g)pteridin-10(2H)-yl)-, DTXCID401777, Isoalloxazine, 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)-, RIBOFLAVIN (II), RIBOFLAVIN [II], RIBOFLAVIN (MART.), RIBOFLAVIN [MART.], 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-D-ribitol, RIBOFLAVIN (USP-RS), RIBOFLAVIN [USP-RS], Riboflavine [INN-French], Riboflavinum [INN-Latin], Riboflavina [INN-Spanish], 7,8-DIMETHYL-10-(1'-D-RIBITYL)ISOALLOXAZINE, RIBOFLAVIN (EP MONOGRAPH), RIBOFLAVIN [EP MONOGRAPH], RIBOFLAVIN (USP MONOGRAPH), RIBOFLAVIN [USP MONOGRAPH], (?)-Riboflavin, 1-Deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo(g)pteridin-10(2H)-yl)pentitol, Benzo(g)pteridine-2,4(3H,10H)-dione, 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)-, 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)benzo[g]pteridine-2,4(3H,10H)-dione, 7,8-dimethyl-10-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-2H,3H,4H,10H-benzo[g]pteridine-2,4-dione, Vitamin B 2, Riboflavin [USP:INN:BAN], vitaminum b2, 1kyv, 2ccb, 2vxa, ()-Riboflavin, 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo(g)pteridin-10(2H)-yl)-D-ribitol, 5-deoxy-5-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo(g)pteridin-10(2H)-yl)-D-ribitol, 5-deoxy-5-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-D-ribitol, 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)benzo(g)pteridine-2,4(3H,10H)-dione, San Yellow B, CAS-83-88-5, NCGC00017291-05, Bisulase (TN), 7,8-dimethyl-10-((2S,3S,4R)-2,3,4,5-tetrahydroxypentyl)benzo(g)pteridine-2,4(3H,10H)-dione, Food Yellow 15, Prestwick_442, Riboflavin (Standard), 2fl5, 2vx9, 4d1y, RIBOFLAVIN [MI], RIBOFLAVIN [FCC], RIBOFLAVIN [INN], RIBOFLAVIN [JAN], Vitamin B2; E101, Prestwick3_000634, RIBOFLAVIN [HSDB], RIBOFLAVIN [VANDF], Epitope ID:161730, RIBOFLAVINUM [HPUS], SCHEMBL7706, CHEMBL1534, RIBOFLAVIN [WHO-DD], RIBOFLAVIN [WHO-IP], VITAMIN B2 [VANDF], BSPBio_000628, MLS001066391, BPBio1_000692, GTPL6578, Riboflavin (JP18/USP/INN), RIBOFLAVINE; VITAMIN B2, RIBOFLAVIN [ORANGE BOOK], HY-B0456R, A11HA04, S01XA26, VITAMIN B2 [GREEN BOOK], 1-deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo(g)pteridin-10(2H)-yl)pentitol, (-)-Riboflavin, 97-103%, HMS2096P10, Benzo[g]pteridine riboflavin deriv., HY-B0456, Riboflavin(B2);7,8-Dimethyl-10-((2S,3S,4R)-2,3,4,5-tetrahydroxypentyl)benzo[g]pteridine-2,4(3H,10H)-dione, RIBOFLAVINUM [WHO-IP LATIN], Tox21_110813, Tox21_111714, Tox21_201633, Tox21_302980, 6,7-Dimethyl-9-ribitylisoalloxazine, BDBM50362895, s2540, Riboflavin (B2), analytical standard, Tox21_111714_1, DB00140, NCGC00091288-01, NCGC00091288-02, NCGC00091288-03, NCGC00091288-04, NCGC00091288-05, NCGC00179498-01, NCGC00256408-01, NCGC00259182-01, AS-15936, SMR000112236, R0020, (-)-Riboflavin, tested according to Ph.Eur., C00255, D00050, EN300-6477227, (-)-Riboflavin, meets USP testing specifications, A840676, Q130365, (-)-Riboflavin, from Eremothecium ashbyii, >=98%, W-104132, BRD-K92760278-001-06-5, BRD-K92760278-001-07-3, Z2216887959, RIBOFLAVIN SODIUM PHOSPHATE IMPURITY D [EP IMPURITY], Riboflavin, European Pharmacopoeia (EP) Reference Standard, Riboflavin, United States Pharmacopeia (USP) Reference Standard, 7,8-Dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)-isoalloxazine, benzo[g]pteridine-2,4(3H,10H)-dione, 7,8-dimethyl-10-ribityl-, Riboflavin, Pharmaceutical Secondary Standard; Certified Reference Material, 3,10-Dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)benzopteridine-2,4-dione, 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)-Benzo[g]pteridine-2,4(3H,10H)-dione, d-ribitol, 1-Deoxy-1-(3,4-dihydro-7,8-dimethyl-2,4-dioxobenzo(g)pteridin-10(-2H)-yl)-, Riboflavin for peak identification, European Pharmacopoeia (EP) Reference Standard, (-)-Riboflavin, 100 mug/mL (1% ammonium acetate in 50:50 methanol:water), certified reference material, ampule of 1 mL, (-)-Riboflavin, BioReagent, suitable for cell culture, suitable for insect cell culture, >=98%, 7,8-dimethyl-10-[(2S,3S,4R)-2,3,4,5-tetrakis(oxidanyl)pentyl]benzo[g]pteridine-2,4-dione, 7,8-dimethyl-2,4-dioxo-10-(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl-2H,3H,4H,10H-benzo[g] vitasanb2;xypentyl)-;E 101;Riboflavin (1.07609);Riboflavin Vitamin B2;Vitamin B2 (Riboflavine);RIBOFLAVIN DC GRADE;RIBOFLAVIN USP (VITAMIN B-2)
Riboflavin may be prevented or treated by oral supplements or by injections.
As a water-soluble vitamin, any riboflavin consumed in excess of nutritional requirements is not stored; it is either not absorbed or is absorbed and quickly excreted in urine, causing the urine to have a bright yellow tint.
Natural sources of riboflavin include meat, fish and fowl, eggs, dairy products, green vegetables, mushrooms, and almonds.
Some countries require its addition to grains.
In its purified, solid form, it is a water-soluble yellow-orange crystalline powder.
Industrial synthesis of riboflavin was initially achieved using a chemical process, but current commercial manufacturing relies on fermentation methods using strains of fungi and genetically modified bacteria.
Riboflavin is moderately soluble in water (10–13 mg/dl) and ethanol but insoluble in ether, chloroform, and acetone.
It is soluble but unstable under alkaline conditions.
The catalytic functions of riboflavin are carried out primarily at positions N-1, N-5, and C-4 of the isoalloxazine nucleus.
In addition, the methyl group at C-8 participates in covalent bonding with enzyme proteins.
The flavin coenzymes are highly versatile redox cofactors because they can participate in either one- or two electron redox reactions.
Riboflavin antagonists include analogs of the isoalloxazine ring (e.g., diethylri boflavin, dichlororiboflavin) and the ribityl side chain (e.g., d-araboflavin, d gaRiboflavin, 7-ethylriboflavin).
Riboflavin, also known as riboflavin or vitamin B2, is a water-soluble vitamin that plays a crucial role in the body's metabolism.
This vitamin is commonly found in foods such as dairy products, eggs, green leafy vegetables, and fortified cereals.
Riboflavin is often used as a dietary supplement for individuals with a deficiency, as it is vital for overall health and well-being.
Additionally, it has applications in the pharmaceutical industry for its use in various formulations.
Riboflavin in which the hydroxy group at position 5 is substituted by a 7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl moiety.
Riboflavin is a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vege ables, but the richest natural source is yeast.
The free form occurs only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as flavin mononucleotide and flavin-adenine dinucleotide.
The conflicting results were eventually found to be due, in part, to deficiencies in study animals not just of vitamin B2,but also vitamin B3 (niacin), the cause of human forms of pellagra,and/or vitamin B6 (pyridoxine), another cause of dermatitis.
Likewise, treatments with vitamin B2 were inconsistent because the early sources of this vitamin contained otherB vitamins.
Vitamin B2 was eventually isolated from egg whites in 1933 and produced synthetically in 1935.
Riboflavin was officially accepted in 1960; although the term was in common use before then.
In 1966, IUPAC changed it to riboflavin, which is in common use today.
Riboflavin is synthesized by all green plants and by mostbacteria and fungi.
Therefore, Riboflavin is found, at least insmall amounts, in most foods.
Foods that are naturally highin riboflavin include milk and other dairy products, meat, eggs, fatty fish, and dark green vegetables.
Chemically, riboflavin is an N-glycoside of flavin, also known as lumichrome, and the sugar, ribitol.
Flavin is derived from the Latin word flavus for “yellow” because of the yellow color of its crystals and yellow fluorescence under UV light.
Riboflavin is heat stable but easilydegraded by light.
Its systematic names are 7,8-dimethyl-10-ribitylisoalloxazine and 7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)isoalloxazine.
Riboflavin serves as a precursor for the active enzyme cofactors riboflavin 5′-monophosphate (also called flavin mononucleotide or FMN) and flavin adenine dinucleotide (FAD).
Riboflavin deficiency in the diet results in a well-defined syndrome known as ariboflavinosis, Riboflavin exhibits protective effects against tumor development and cardiovascular disease.
Its deficiency often affects metabolism involving redox reactions.
Riboflavin is found essential for iron absorption, gastrointestinal development, neurogenesis, corneal vascularization and corneal opacity.
Severe Riboflavin deficiency is known as ariboflavinosis, and treatment or prevention of this condition is the only provenuse of riboflavin.
Ariboflavinosis is most commonly associated with multiple vitamin deficiency as a result of alcoholism in developed countries.
Because of the large number of enzymes requiring riboflavin as a coenzyme, deficienciescan lead to a wide range of abnormalities.
In adults seborrheicdermatitis, photophobia, peripheral neuropathy, anemia, andoropharyngeal changes including angular stomatitis, glossitis, and cheilosis, are often the first signs of riboflavin deficiency.
In children, cessation of growth can also occur.
As the deficiencyprogresses, more severe pathologies develop until death ensues.
Riboflavin deficiency may also produce teratogeniceffects and alter iron handling leading to anemia.
Riboflavin, also known as vitamin B2, is a water-soluble vitamin and is one of the B vitamins.
Unlike folate and vitamin B6, which occur in several chemically related forms known as vitamers, riboflavin is only one chemical compound.
Riboflavin is a starting compound in the synthesis of the coenzymes flavin mononucleotide (FMN, also known as riboflavin-5'-phosphate) and flavin adenine dinucleotide (FAD).
FAD is the more abundant form of flavin, reported to bind to 75% of the number of flavin-dependent protein encoded genes in the all-species genome (the flavoproteome) and serves as a co-enzyme for 84% of human-encoded flavoproteins.
In its purified, solid form, Riboflavin is a yellow-orange crystalline powder with a slight odor and bitter taste.
Riboflavin is soluble in polar solvents, such as water and aqueous sodium chloride solutions, and slightly soluble in alcohols.
It is not soluble in non-polar or weakly polar organic solvents such as chloroform, benzene or acetone.
In solution or during dry storage as a powder, Riboflavin is heat stable if not exposed to light.
When heated to decompose, it releases toxic fumes containing nitric oxide.
Riboflavin deficiency is uncommon in the United States and in other countries with wheat flour or corn meal fortification programs.
From data collected in biannual surveys of the U.S. population, for ages 20 and over, 22% of women and 19% of men reported consuming a supplement that contained Riboflavin, typically a vitamin-mineral multi-supplement.
For the non-supplement users, the dietary intake of adult women averaged 1.74 mg/day and men 2.44 mg/day.
These amounts exceed the RDAs for riboflavin of 1.1 and 1.3 mg/day respectively.
For all age groups, on average, consumption from food exceeded the RDAs.
Riboflavin deficiency (also called ariboflavinosis) results in stomatitis, symptoms of which include chapped and fissured lips, inflammation of the corners of the mouth (angular stomatitis), sore throat, painful red tongue, and hair loss.
The eyes can become itchy, watery, bloodshot, and sensitive to light.
Riboflavin deficiency is associated with anemia.
Prolonged riboflavin insufficiency may cause degeneration of the liver and nervous system.
Riboflavin deficiency may increase the risk of preeclampsia in pregnant women.
Deficiency of riboflavin during pregnancy can result in fetal birth defects, including heart and limb deformities.
Riboflavin deficiency is usually found together with other nutrient deficiencies, particularly of other water-soluble vitamins.
A deficiency of riboflavin can be primary (i.e. caused by poor vitamin sources in the regular diet) or secondary, which may be a result of conditions that affect absorption in the intestine.
Secondary deficiencies are typically caused by the body not being able to use the vitamin, or by an increased rate of excretion of the vitamin.
Diet patterns that increase risk of deficiency include veganism and low-dairy vegetarianism.
Diseases such as cancer, heart disease and diabetes may cause or exacerbate riboflavin deficiency.
There are rare genetic defects that compromise riboflavin absorption, transport, metabolism or use by flavoproteins.
One of these is riboflavin transporter deficiency, previously known as Brown–Vialetto–Van Laere syndrome.
Variants of the genes SLC52A2 and SLC52A3 which code for transporter proteins RDVT2 and RDVT3, respectively, are defective.
Infants and young children present with muscle weakness, cranial nerve deficits including hearing loss, sensory symptoms including sensory ataxia, feeding difficulties, and respiratory distress caused by a sensorimotor axonal neuropathy and cranial nerve pathology.
When untreated, infants with riboflavin transporter deficiency have labored breathing and are at risk of dying in the first decade of life.
Treatment with oral supplementation of high amounts of riboflavin is lifesaving.
Other inborn errors of metabolism include Riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency, also known as a subset of glutaric acidemia type 2, and the C677T variant of the methylenetetrahydrofolate reductase enzyme, which in adults has been associated with risk of high blood pressure.
The name "riboflavin" comes from "ribose" (the sugar whose reduced form, ribitol, forms part of its structure) and "flavin", the ring-moiety that imparts the yellow color to the oxidized molecule (from Latin flavus, "yellow").
The reduced form, which occurs in metabolism along with the oxidized form, appears as orange-yellow needles or crystals.
The earliest reported identification, predating any concept of vitamins as essential nutrients, was by Alexander Wynter Blyth.
In 1879, Blyth isolated a water-soluble component of cows' milk whey, which he named "lactochrome", that fluoresced yellow-green when exposed to light.
In the early 1900s, several research laboratories were investigating constituents of foods, essential to maintain growth in rats.
These constituents were initially divided into fat-soluble "vitamine" A and water-soluble "vitamine" B. (The "e" was dropped in 1920).
Vitamin B was further thought to have two components, a heat-labile substance called B1 and a heat-stable substance called B2.
Riboflavin was tentatively identified to be the factor necessary for preventing pellagra, but that was later confirmed to be due to niacin (vitamin B3) deficiency.
The confusion was due to the fact that riboflavin (B2) deficiency causes stomatitis symptoms similar to those seen in pellagra, but without the widespread peripheral skin lesions.
For this reason, early in the history of identifying Riboflavin deficiency in humans the condition was sometimes called "pellagra sine pellagra" (pellagra without pellagra).
In 1935, Paul Gyorgy, in collaboration with chemist Richard Kuhn and physician T. Wagner-Jauregg, reported that rats kept on a B2-free diet were unable to gain weight.
Isolation of B2 from yeast revealed the presence of a bright yellow-green fluorescent product that restored normal growth when fed to rats. The growth restored was directly proportional to the intensity of the fluorescence.
This observation enabled the researchers to develop a rapid chemical bioassay in 1933, and then isolate the factor from egg white, calling it ovoflavin.
The same group then isolated the a similar preparation from whey and called it Riboflavin.
In 1934, Kuhn's group identified the chemical structure of these flavins as identical, settled on "riboflavin" as a name, and were also able to synthesize the vitamin.
In 1938, Richard Kuhn was awarded the Nobel Prize in Chemistry for his work on vitamins, which had included B2 and B6.
Riboflavin was confirmed that riboflavin is essential for human health through a clinical trial conducted by William H. Sebrell and Roy E. Butler.
Women fed a diet low in riboflavin developed stomatitis and other signs of deficiency, which were reversed when treated with synthetic Riboflavin.
The symptoms returned when the supplements were stopped.
As a water-soluble vitamin, it is involved in many metabolic processes in the human body.
Riboflavin is therefore found in every single cell of the body.
It plays a particularly important role in the conversion of carbohydrates, protein and fat into nutrients.
Riboflavin can influence human growth and, in combination with vitamin A, support the repair of the body’s own tissue.
In cosmetics, the vitamin is very often used to treat flaky, dry skin.
Riboflavin is involved in the chemical regeneration of the enzyme glutathione, which is primarily responsible for protecting against possible damage from the dreaded free radicals.
A deficiency of this vitamin can manifest itself in several ways.
Those affected often feel tired and lethargic, often the immune system is weakened or there is an increased sensitivity to light.
External signs are mainly a waxy appearance of the skin in connection with scaly and very dry areas.
Very typical are also cracked corners of the mouth, which are often very painful.
In addition to its function as a vitamin, it is used as a food coloring agent.
Biosynthesis takes place in bacteria, fungi and plants, but not animals.
Riboflavin is essential for the production of energy, as it helps convert carbohydrates, fats, and proteins into usable energy within the cells.
Melting point: 290 °C (dec.)(lit.)
alpha: -135 º (c=5, 0.05 M NaOH)
Boiling point: 504.93°C (rough estimate)
Density: 1.2112 (rough estimate)
Bulk density: 100kg/m3
Refractive index: -135 ° (C=0.5, JP Method)
Flash point: 9℃
Storage temp.: 2-8°C
Solubility: Very slightly soluble in water, practically insoluble in ethanol (96 per cent). Solutions deteriorate on exposure to light, especially in the presence of alkali. It shows polymorphism (5.9).
Form: Powder
pKa: 1.7(at 25℃)
Color: Yellow to orange
pH: 5.5-7.2 (0.07g/l, H2O, 20°C)
Odor: Slight odour
pH Range: 6
Optical activity: [α]/D -135.0 to -155.0°, c =0.5% in 0.05 M NaOH (dry basis)
Biological source: Synthetic
Water Solubility: 0.07 g/L (20 ºC)
Sensitive: Light Sensitive
Merck: 14,8200
BRN: 97825
BCS Class: 1
Stability: Stable, but light-sensitive. Incompatible with strong oxidizing agents, reducing agents, bases, calcium, metallic salts. May be moisture sensitive.
InChIKey: AUNGANRZJHBGPY-SCRDCRAPSA-N
LogP: -2.009 (est)
In the early 1930s, several groups found the coenzyme forms of riboflavin 50-phosphate (flavin mononucleotide) and the further conjugate with adenylic acid (flavin adenine dinucleotide).
Some earlier designations for this substance included vitamin G, Riboflavin, hepatoflavin, ovoflavin, verdoflavin.
The chemical name is 6,7-dimethyl-9-d-l’ribityl isolloxazine.
Riboflavin is a complex pigment with a green fluorescence.
Riboflavin, also known as vitamin B2, is a vitamin found in food and sold as a dietary supplement.
Riboflavin is essential to the formation of two major coenzymes, flavin mononucleotide and flavin adenine dinucleotide.
Riboflavin is essential to the formation of two major coenzymes, FMN and FAD.
These coenzymes are involved in energy metabolism, cell respiration, antibody production, growth and development.
Riboflavin is essential for the metabolism of carbohydrates, protein and fats.
FAD contributes to the conversion of tryptophan to niacin (vitamin B3) and the conversion of vitamin B6 to the coenzyme pyridoxal 5'-phosphate requires FMN.
Riboflavin is involved in maintaining normal circulating levels of homocysteine; in riboflavin deficiency, homocysteine levels increase, elevating the risk of cardiovascular diseases.
Redox reactions are processes that involve the transfer of electrons.
The flavin coenzymes support the function of roughly 70-80 flavoenzymes in humans (and hundreds more across all organisms, including those encoded by archeal, bacterial and fungal genomes) that are responsible for one- or two-electron redox reactions which capitalize on the ability of flavins to be converted between oxidized, half-reduced and fully reduced forms.
FAD is also required for the activity of glutathione reductase, an essential enzyme in the formation of the endogenous antioxidant, glutathione.
Biosynthesis takes place in bacteria, fungi and plants, but not animals.
The biosynthetic precursors to riboflavin are ribulose 5-phosphate and guanosine triphosphate.
The former is converted to L-3,4-dihydroxy-2-butanone-4-phosphate while the latter is transformed in a series of reactions that lead to 5-amino-6-(D-ribitylamino)uracil.
These two compounds are then the substrates for the penultimate step in the pathway, catalysed by the enzyme lumazine synthase in reaction.
In the final step of the biosynthesis, two molecules of 6,7-dimethyl-8-ribityllumazine are combined by the enzyme riboflavin synthase in a dismutation reaction.
This generates one molecule of riboflavin and one of 5-amino-6-(D-ribitylamino) uracil.
The latter is recycled to the previous reaction in the sequence.
The industrial-scale production of riboflavin uses various microorganisms, including filamentous fungi such as Ashbya gossypii, Candida famata and Candida flaveri, as well as the bacteria Corynebacterium ammoniagenes and Bacillus subtilis.
B. subtilis that has been genetically modified to both increase the production of riboflavin and to introduce an antibiotic (ampicillin) resistance marker, is employed at a commercial scale to produce riboflavin for feed and food fortification.
By 2012, over 4,000 tonnes per annum were produced by such fermentation processes.
In the presence of high concentrations of hydrocarbons or aromatic compounds, some bacteria overproduce riboflavin, possibly as a protective mechanism.
One such organism is Micrococcus luteus (American Type Culture Collection strain number ATCC 49442), which develops a yellow color due to production of riboflavin while growing on pyridine, but not when grown on other substrates, such as succinic acid.
Keratoconus is the most common form of corneal ectasia, a progressive thinning of the cornea.
The condition is treated by corneal collagen cross-linking, which increases corneal stiffness.
Cross-linking is achieved by applying a topical riboflavin solution to the cornea, which is then exposed to ultraviolet A light.
In its 2012 guidelines, the American Academy of Neurology stated that high-dose Riboflavin (400 mg) is "probably effective and should be considered for migraine prevention," a recommendation also provided by the UK National Migraine Centre.
A 2017 review reported that daily riboflavin taken at 400 mg per day for at least three months may reduce the frequency of migraine headaches in adults.
Research on high-dose riboflavin for migraine prevention or treatment in children and adolescents is inconclusive, and so supplements are not recommended.
The white flour produced after milling of wheat has only 67% of its original riboflavin amount left, so white flour is enriched in some countries.
Riboflavin is also added to ready-to-eat breakfast cereals.
Riboflavin is difficult to incorporate riboflavin into liquid products because it has poor solubility in water, hence the requirement for riboflavin-5'-phosphate (FMN, also called E101 when used as colorant), a more soluble form of riboflavin.
The enrichment of bread and ready-to-eat breakfast cereals contributes significantly to the dietary supply of the vitamin.
Free riboflavin is naturally present in animal-sourced foods along with protein-bound FMN and FAD. Cows' milk contains mainly free riboflavin, but both FMN and FAD are present at low concentrations.
Riboflavin, or riboflavin, is a member of the B-vitamin complex and is water-soluble, meaning it is not stored in the body and must be regularly replenished through diet or supplements.
It plays a fundamental role in the electron transport chain, a key process in cellular respiration, by helping convert food into energy.
This vitamin also aids in the synthesis of important molecules like coenzymes FAD (flavin adenine dinucleotide) and FMN (flavin mononucleotide), which are essential for a variety of metabolic processes, including the metabolism of amino acids and fatty acids.
As a powerful antioxidant, Riboflavin helps neutralize harmful free radicals, reducing oxidative stress in the body.
This contributes to the maintenance of cell integrity, skin health, and proper function of the immune system.
Additionally, riboflavin is essential for the maintenance of healthy vision, as it helps prevent cataracts and other eye conditions that can arise from vitamin deficiencies.
Deficiency in Riboflavin can lead to a condition called ariboflavinosis, which is characterized by symptoms such as sore throat, cracks or sores on the lips (cheilosis), inflammation and redness of the tongue (glossitis), and an overall lack of energy.
Riboflavin is often found in conjunction with other vitamin deficiencies, particularly in populations with poor diets or limited access to dairy products, eggs, and leafy greens.
In the pharmaceutical and cosmetic industries, Riboflavin is frequently used as an ingredient in skin care formulations due to its potential for promoting wound healing and reducing inflammation.
Furthermore, it is sometimes used in the production of food products as a coloring agent, particularly in the form of a yellow dye (E101), known for its bright yellow hue and antioxidant properties.
Riboflavin, which is only moderately water soluble, is absorbed from the gastrointestinal tract but is limited to about 27 mg at any one time from an oral dose given to an adult. Hence, mega doses would not be expected to increase significantly the total amount absorbed.
Riboflavin is hepatically metabolized, protein bound, and widely distributed to tissue; however, little is stored in the liver, spleen, heart, and kidneys.
Riboflavin is excreted renally as metabolites, which have been oxidatively cleaved in the ribityl side chain and converted to hydroxymethyls in the ring methyl functions.
Riboflavin in excess of daily body needs is excreted unchanged in the urine.
Riboflavin exhibits biphasic pharmacokinetics with initial and terminal half-lives of 1.4 and 14 h, respectively.
Riboflavin is absorbed by the small intestine, it is quickly removed from the blood and excreted in urine.
Urine color is used as a hydration status biomarker and, under normal conditions, correlates with urine specific gravity and urine osmolality.
However, riboflavin supplementation in large excess of requirements causes urine to appear more yellow than normal.
With normal dietary intake, about two-thirds of urinary output is riboflavin, the remainder having been partially metabolized to hydroxymethyl riboflavin from oxidation within cells, and as other metabolites.
When consumption exceeds the ability to absorb, riboflavin passes into the large intestine, where it is catabolized by bacteria to various metabolites that can be detected in feces.
There is speculation that unabsorbed riboflavin could affect the large intestine microbiome.
These coenzymes are involved in energy metabolism, cellular respiration, and antibody production, as well as normal growth and development.
The coenzymes are also required for the metabolism of niacin, vitamin B6, and folate.
Riboflavin is involved in numerous enzymatic reactions that support the maintenance of healthy skin, eyes, and the nervous system.
Riboflavin also has antioxidant properties, protecting cells from oxidative damage caused by free radicals.
Uses of Riboflavin:
Riboflavin is used in the production of supplements that help prevent or treat riboflavin deficiency.
Riboflavin is often included in multivitamin formulations or as a stand-alone supplement, particularly for individuals who may have dietary restrictions or conditions that impair nutrient absorption.
It is also used in the treatment of certain health conditions, such as migraines and cataracts, as riboflavin has been shown to play a role in reducing the frequency and severity of migraines, as well as in supporting eye health.
Riboflavin is incorporated into products aimed at improving skin health.
Due to its antioxidant properties, it is often added to creams, lotions, and ointments designed to protect the skin from environmental damage, reduce inflammation, and promote healing.
Riboflavin has also been found to be beneficial in the treatment of certain skin conditions, such as acne and eczema, as it helps to reduce irritation and promote tissue repair.
Riboflavin is used in scientific and medical research.
It is studied for its potential therapeutic benefits, including its role in cellular energy production and its impact on the immune system.
Researchers are also investigating its antioxidant properties and its ability to protect against oxidative stress, which is linked to the development of various chronic diseases.
Riboflavin, or riboflavin, also finds applications in the agricultural industry, particularly in animal nutrition.
It is commonly included in animal feed formulations to ensure that livestock, poultry, and other farm animals receive sufficient amounts of this essential nutrient.
Riboflavin is critical for the proper growth, metabolism, and overall health of animals, as it plays a vital role in energy production and cell function.
Deficiencies in Riboflavin can lead to growth retardation, reproductive issues, and other health problems in animals, so its inclusion in animal feed is an important measure for maintaining livestock health and productivity.
In the realm of biotechnology, Riboflavin is used as a coenzyme in various enzymatic processes.
Because of its ability to facilitate oxidative reactions, riboflavin is incorporated into research processes that require redox reactions.
Riboflavin is often used in laboratory studies where enzymes that utilize riboflavin as a cofactor are studied for industrial or medical applications.
This includes its use in fermentation processes for the production of biofuels, pharmaceuticals, and other bio-based products.
In the pharmaceutical industry, Riboflavin is also involved in certain medical treatments.
For instance, riboflavin is used in the treatment of specific genetic disorders, such as mitochondrial myopathies, where it supports cellular metabolism and energy production.
Riboflavin supplementation can improve the quality of life for individuals with these rare conditions, as it helps optimize the function of mitochondria—the powerhouses of cells.
Riboflavin is part of the research into its role in reducing the risk of certain cancers and cardiovascular diseases.
Studies suggest that adequate riboflavin levels may lower the risk of certain types of cancer, such as those affecting the mouth, throat, and skin, by enhancing the body's ability to repair damaged cells.
Riboflavin also helps in the regulation of homocysteine levels in the blood, an amino acid that, in elevated levels, is associated with an increased risk of heart disease.
This property makes riboflavin a subject of interest in cardiovascular health research.
Riboflavin is sometimes incorporated into certain wound-healing treatments.
Topical applications of Riboflavin have been explored for their ability to promote wound healing and tissue regeneration.
Some studies have shown that Riboflavin can accelerate the healing process for superficial cuts, abrasions, and burns by stimulating collagen production and supporting the skin's natural healing mechanisms.
Riboflavin plays a role in enhancing the efficacy of other vitamins and nutrients.
It is often included in combination supplements with other B vitamins, as it works synergistically with them to improve energy production, maintain healthy skin, and support nerve function.
Its interaction with folic acid, in particular, is crucial for the synthesis of red blood cells and the proper functioning of the nervous system.
This makes it an essential component in multivitamin supplements designed to promote overall health and well-being.
Riboflavin is produced by yeast from glucose, urea, and mineral salts in an aerobic fermentation.
Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables.
Richest natural source is yeast.
Minute amounts present in all plant and animal cells.
Vitamin B2; Vitamin cofactor; LD50(rat) 560 mg/kg ip
Riboflavin is used in skin care preparations as an emollient.
Riboflavin can be found in sun care products as a suntan enhancer.
Medicinally, it is used for the treatment of skin lesions.
Riboflavin is the water-soluble vitamin b2 required for healthy skin and the building and maintaining of body tissues.
Riboflavin is a yellow to orange-yellow crystalline powder.
Riboflavin acts as a coenzyme and carrier of hydrogen.
Riboflavin is stable to heat but may dissolve and be lost in cooking water.
Riboflavin is relatively stable to storage.
Sources include leafy vegetables, cheese, eggs, and milk.
Riboflavin, also known as riboflavin, is widely utilized in both the food and pharmaceutical industries due to its essential role in various biological processes.
In the food industry, it is primarily used as a food additive and coloring agent, where it is often labeled as E101.
It imparts a yellow color to products such as beverages, dairy products, and certain baked goods.
The addition of Riboflavin in these products not only enhances their visual appeal but also serves to fortify the food with an essential nutrient, ensuring that consumers receive an adequate intake of this vital vitamin.
In addition to its use as a coloring agent, Riboflavin plays a critical role in the fortification of foods and dietary supplements.
It is commonly added to breakfast cereals, infant formulas, and other processed foods to prevent riboflavin deficiency, which can lead to health problems such as ariboflavinosis.
By supplementing the diet with Riboflavin, manufacturers help to address potential nutrient gaps and support overall health and wellness.
Safety Profile Of Riboflavin:
Riboflavin, or riboflavin, is generally considered to be safe when used in appropriate quantities, but there are a few potential hazards and precautions associated with its use, particularly at higher concentrations or in certain sensitive individuals.
One of the primary concerns with Riboflavin is its potential for causing allergic reactions, although these are relatively rare.
Some individuals may experience symptoms such as skin rashes, itching, or swelling after exposure to riboflavin or products containing it, particularly if they have a sensitivity to vitamins or certain additives used in the formulation.
Severe allergic reactions, including difficulty breathing and anaphylaxis, are extremely uncommon but can occur in highly sensitive individuals.
Ingestion of excessive amounts of Riboflavin is unlikely to lead to serious adverse effects because it is a water-soluble vitamin, meaning that excess amounts are typically excreted through urine.
However, in very high doses, riboflavin may cause minor gastrointestinal discomfort, such as nausea or diarrhea.
While riboflavin toxicity is rare, it’s important to follow recommended dosage guidelines, especially when taking riboflavin supplements, to avoid unnecessary side effects.
In humans, there is no evidence for riboflavin toxicity produced by excessive intakes and absorption becomes less efficient as dosage increases.
Any excess riboflavin is excreted via the kidneys into urine, resulting in a bright yellow color known as flavinuria.
During a clinical trial on the effectiveness of riboflavin for treating the frequency and severity of migraines, subjects were given up to 400 mg of riboflavin orally per day for periods of 3–12 months.
Abdominal pains and diarrhea were among the side effects reported.
Poison by intravenous route moderately toxic by intraperitoneal and subcutaneous routes.
Mutation data reported. When heated to decomposition it emits toxic fumes of NOx.
