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===Metabolism and excretion===
===Metabolism and excretion===
Biotin catabolism occurs via two pathways. In one, the valeric acid sidechain is cleaved, resulting in bisnorbiotin. In the other pathway, the sulfur is oxidized, resulting in biotin sulfoxide. Urine content is proportionally about half biotin, plus bisnorbiotin, biotin sulfoxide and small amounts of other metabolites.<ref name=PKIN2020Biotin />
Biotin [[catabolism]] occurs via two pathways. In one, the valeric acid sidechain is cleaved, resulting in bisnorbiotin. In the other pathway, the sulfur is oxidized, resulting in biotin sulfoxide. Urine content is proportionally about half biotin, plus bisnorbiotin, biotin sulfoxide and small amounts of other metabolites.<ref name=PKIN2020Biotin />


===Factors that affect biotin requirements===
===Factors that affect biotin requirements===

Revision as of 22:24, 6 February 2021

Biotin
Skeletal formula of biotin
Ball-and-stick model of the Biotin molecule
Names
IUPAC name
5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoic acid
Other names
Vitamin B7; Vitamin H; Coenzyme R; Biopeiderm
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.000.363 Edit this at Wikidata
KEGG
UNII
  • InChI=1S/C10H16N2O3S/c13-8(14)4-2-1-3-7-9-6(5-16-7)11-10(15)12-9/h6-7,9H,1-5H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1 checkY
    Key: YBJHBAHKTGYVGT-ZKWXMUAHSA-N checkY
  • InChI=1/C10H16N2O3S/c13-8(14)4-2-1-3-7-9-6(5-16-7)11-10(15)12-9/h6-7,9H,1-5H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1
    Key: YBJHBAHKTGYVGT-ZKWXMUAHBB
  • O=C1N[C@@H]2[C@@H](SC[C@@H]2N1)CCCCC(=O)O
  • C1[C@H]2[C@@H]([C@@H](S1)CCCCC(=O)O)NC(=O)N2
Properties
C10H16N2O3S
Molar mass 244.31 g·mol−1
Appearance White crystalline needles
Melting point 232 to 233 °C (450 to 451 °F; 505 to 506 K)
22 mg/100 mL
Pharmacology
A11HA05 (WHO)
Hazards
NFPA 704 (fire diamond)
NFPA 704 four-colored diamondHealth 1: Exposure would cause irritation but only minor residual injury. E.g. turpentineFlammability 1: Must be pre-heated before ignition can occur. Flash point over 93 °C (200 °F). E.g. canola oilInstability 0: Normally stable, even under fire exposure conditions, and is not reactive with water. E.g. liquid nitrogenSpecial hazards (white): no code
1
1
0
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
checkY verify (what is checkY☒N ?)

Biotin, also called vitamin B7, is one of the B vitamins.[1][2][3] It is involved in a wide range of metabolic processes, both in humans and in other organisms, primarily related to the utilization of fats, carbohydrates, and amino acids.[4] The name biotin derives from the Greek word “bios” (to live) and the suffix “-in” (a general chemical suffix used in organic chemistry).[5]

Biotin deficiency can be caused by inadequate dietary intake (rare) or inheritance of one or more inborn genetic disorders that affect biotin metabolism. The most common among these is biotinidase deficiency. Low activity of this enzyme causes a failure to recycle biotin from biocytin. Rarer are carboxylase and biotin transporter deficiences.[4][6] Subclinical deficiency can cause mild symptoms, such as hair thinning, brittle fingernails, or skin rash, typically on the face.[2][4] Neonatal screening for biotinidase deficiency started in the United States in 1984, with many countries now also testing for this genetic disorder at birth. Treatment is lifelong dietary supplement with biotin.[1]

Definition

Biotin is a water-soluble B-vitamin. It is composed of a ureido ring fused with a tetrahydrothiophene ring. The ureido ring containing the –N–CO–N– group acts as the carbon dioxide carrier in carboxylation reactions.[7] A valeric acid substituent is attached to one of the carbon atoms of the tetrahydrothiophene ring. Biotin is a coenzyme for five carboxylase enzymes, which are involved in the digestion of carbohydrates, synthesis of fatty acids, and gluconeogenesis.[3][4] Biotinylation of histone proteins in nuclear chromatin plays a role in chromatin stability and gene expression.[4][8]

Dietary recommendations

The US National Academy of Medicine updated Dietary Reference Intakes for many vitamins in 1998. At that time there was insufficient information to establish estimated average requirement or recommended dietary allowance, terms that exist for most vitamins. In instances such as this, the Academy sets adequate intakes (AIs) with the understanding that at some later date, when the physiological effects of biotin are better understood, AIs will be replaced by more exact information. The biotin AIs for both males and females are: 5 μg/day of biotin for 0-6-month-olds, 6 μg/day of biotin for 7-12-month-olds, 8 μg/day of biotin for 1-3-year-olds, 12 μg/day of biotin for 4-8-year-olds, 20 μg/day of biotin for 9-13-year-olds, 25 μg/day of biotin for 14-18-year-olds, and 30 μg/day of biotin for those 19-years old and older. The biotin AIs for females who are either pregnant or lactating, respectively, are: 30 μg/day of biotin for pregnant females 14-50-years old; 35 μg/day of biotin for lactating females 14-50-years old.[2] Australia and New Zealand set AIs similar to the US.[9]

The European Food Safety Authority (EFSA) also identifies AIs, setting values at 40 μg/day for adults, pregnancy at 40 μg/day, and breastfeeding at 45 μg/day. For children ages 1–17 years, the AIs increase with age from 20 to 35 μg/day.[10]

Safety

The US National Academy of Medicine estimates upper limits (ULs) for vitamins and minerals when evidence for a true limit is sufficient. For biotin, however, there is no UL because adverse effects of high biotin intake have not been determined.[2] The EFSA also reviewed safety and reached the same conclusion as in the United States.[11]

Labeling regulations

For US food and dietary supplement labeling purposes the amount in a serving is expressed as a percent of daily value. For biotin labeling purposes 100% of the daily value was 300 μg/day, but as of May 27, 2016 it was revised to 30 μg/day to bring it into an agreement with the adequate intake.[12][13] Compliance with the updated labeling regulations was required by 1 January 2020 for manufacturers with US$10 million or more in annual food sales, and by 1 January 2021 for manufacturers with lower volume food sales.[14][15] A table of the old and new adult daily values is provided at Reference Daily Intake.

Sources

Sources with appreciable content are:

Source[16] Amount
(μg / 100 g)
Chicken liver 187
Beef liver 42
Eggs 21
Egg white 5.8
Egg yolk 27
Salmon, canned in water 5.9
Pork chop 4.5
Turkey breast 0.7
Tuna, white, canned 0.7
Source[16] Amount
(μg / 100 g)
Peanuts, roasted 17.5
Sunflower seeds, roasted 7.8
Almonds, roasted 4.4
Sweet potato 1.5
Broccoli 0.9
Tomato 0.7
Strawberry 1.5
Avocado 1.0
Corn, canned 0.05
Source[16] Amount
(μg / 100 g)
Cheese 1.4
Milk 0.1
Corn flakes cereal 0.1
Oatmeal 0.1
Bread 0.1
French fries 0.3
Wine 0.1
Beer 0.1
Potatos, mashed 0.1

Biotin is stable at room temperature and is not destroyed by cooking. The dietary biotin intake in Western populations has been estimated to be in the range of 35 to 70 μg/day. Nursing infants ingest about 6 μg/day.[4] Biotin is available in dietary supplements, individually or as an ingredient in multivitamins.[1][3]

No government fortification programs

According to the Global Fortification Data Exchange, biotin deficiency is so rare that no countries require that foods be fortified.[17]

Physiology

Biotin is a water-soluble B vitamin. Consumption of large amounts as a dietary supplement results in absorption, followed by excretion into urine as biotin. Consumption of biotin as part of a normal diet results in urinary excretion of biotin and biotin metabolites.

Absorption

Biotin in food is bound to proteins. Digestive enzymes reduce the proteins to biotin-bound peptides. The intestinal enzyme biotinidase, found in pancreatic secretions and in the brush border membranes of all three parts of the small intestine, frees biotin, which is then absorbed from the small intestine.[4] When consumed as a biotin dietary supplement, absorption is nonsaturable, meaning that even very high amounts are absorbed effectively. Transport across the jejunum is faster than across the ileum.[4]

The large intestine microbiota synthesize amounts of biotin estimated to be similar to the amount taken in the diet, and a significant portion of this biotin exists in the free (protein-unbound) form and, thus, is available for absorption. How much is absorbed in humans is unknown, although a review did report that human epithelial cells of the colon in vitro demonstrated an ability to update biotin.[18]

Once absorbed, sodium-dependent multivitamin transporter (SMVT) mediates biotin uptake into the liver.[4] SMVT also binds pantothenic acid, so high intakes of either of these vitamins can interfere with transport of the other.[19]

Metabolism and excretion

Biotin catabolism occurs via two pathways. In one, the valeric acid sidechain is cleaved, resulting in bisnorbiotin. In the other pathway, the sulfur is oxidized, resulting in biotin sulfoxide. Urine content is proportionally about half biotin, plus bisnorbiotin, biotin sulfoxide and small amounts of other metabolites.[4]

Factors that affect biotin requirements

Chronic alcohol use is associated with a significant reduction in plasma biotin.[20] Intestinal biotin uptake also appears to be sensitive to the effect of the anti-epilepsy drugs carbamazepine and primidone.[20] Relatively low levels of biotin have also been reported in the urine or plasma of patients who have had a partial gastrectomy or have other causes of achlorhydria, burn patients, elderly individuals, and athletes.[21] Pregnancy and lactation may be associated with an increased demand for biotin. In pregnancy, this may be due to a possible acceleration of biotin catabolism, whereas, in lactation, the higher demand has yet to be elucidated. Recent studies have shown marginal biotin deficiency can be present in human gestation, as evidenced by increased urinary excretion of 3-hydroxyisovaleric acid, decreased urinary excretion of biotin and bisnorbiotin, and decreased plasma concentration of biotin.[4]

Biosynthesis

Biotin is a heterocyclic, sulfur-containing monocarboxylic acid with two rings fused together via one of their sides (figure). The two rings are ureido and tetrahydrothiophene moieties.[22] Biotin, synthesized in plants, is essential to plant growth and development.[23] Synthesis starts from two precursors, alanine and pimeloyl-CoA. These form 7-Keto-8-aminopelargonic acid (KAPA). KAPA is transported from plant peroxisomes to mitochondria where it is converted to 7,8-Diaminopelargonic acid (DAPA). The enzyme dethiobiotin synthetase catalyzes the formation of the ureido ring via a DAPA carbamate activated with ATP, creating dethiobiotin. The last step is catalyzed by biotin synthase.[22][23]

Cofactor biochemistry

The enzyme holocarboxylase synthetase covalently attaches biotin to five human carboxylase enzymes:[4]

For the first two, biotin serves as a cofactor responsible for transfer of bicarbonate to acetyl-CoA, converting it to malonyl-CoA for fatty acid synthesis. PC participates in gluconeogenesis. MCC catalyzes a step in leucine metabolism. PCC catalyzes a step in the metabolism of propionyl-CoA.[1][3][4] Metabolic degradation of the biotinylated carboxylases leads to the formation of biocytin. This compound is further degraded by biotinidase to release biotin, which is then reutilized by holocarboxylase synthetase.[4]

In addition to carboxylase functions, biotinylation of histone proteins in nuclear chromatin plays a role in chromatin stability and gene expression.[4][8]

Deficiency

Main article: Biotin deficiency

Biotin deficiency in humans is rare. Signs of biotin deficiency have been described in people who were receiving all nutrition intravenously without biotin, also people regularly consuming raw or incompletely cooked egg whites, because egg whites contain avidin, a biotin-binding protein. Deficiency symptoms include: brittle and thin fingernails, hair loss (alopecia), conjunctivitis, dermatitis in the form of a scaly, red rash around the eyes, nose, mouth, and genital area, plus neurological symptoms such as depression, lethargy, hallucination, and numbness and tingling of the extremities[4] The neurological and psychological symptoms can occur with only mild deficiencies. Dermatitis, conjunctivitis, and hair loss will generally occur only when deficiency becomes more severe. Individuals with hereditary disorders of biotin deficiency have evidence of impaired immune system function, including increased susceptibility to bacterial and fungal infections.[3]

Diagnosis

Low serum and urine biotin are not sensitive indicators of inadequate biotin intake.[4] However, serum testing can be useful for confirmation of consumption of biotin-containing dietary supplements, and whether a period of refraining from supplement use is long enough to eliminate the potential for interfering with drug tests.[24][25] Indirect measures depend on the biotin requirement for carboxylases. 3-Methylcrotonyl-CoA is an intermediate step in the catabolism of the amino acid leucine. In the absence of biotin, the pathway diverts to 3-hydroxyisovaleric acid. Urinary excretion of this compound is an early and sensitive indicator of biotin deficiency.[2][4]

Metabolic disorders

Biotinidase deficiency is a deficiency of the enzyme that recycles biotin, the consequence of an inherited genetic mutation.[1] Biotinidase catalyzes the cleavage of biotin from biocytin and biotinyl-peptides (the proteolytic degradation products of each holocarboxylase) and thereby recycles biotin.[2] It is also important in freeing biotin from dietary protein-bound biotin.[26] Other inherited metabolic disorders characterized by deficient activities of biotin-dependent carboxylases are termed multiple carboxylase deficiency. These include deficiencies in the enzymes holocarboxylase synthetase or biotinidase.[1] Holocarboxylase synthetase deficiency prevents the body's cells from using biotin effectively and thus interferes with multiple carboxylase reactions.[26] Biochemical and clinical manifestations include ketolactic acidosis, organic aciduria, hyperammonemia, skin rash, feeding problems, hypotonia, seizures, developmental delay, alopecia, and coma.

Prevalence, diagnosis and treatment

Profound biotinidase deficiency, defined as less than 10% of normal serum enzyme activity, which has been reported as 7.1 nmol/min/mL, has an incidence of 1 in 40,000 to 1 in 60,000, but with rates as high as 1 in 10,000 in countries with high incidence of consanguineous marriages (second cousin or closer). Partial biotinidase deficiency is defined as 10% to 30% of normal serum activity.[27] Incidence data stems from government mandated newborn screening, which as of 2017 was reported as required in more than 30 countries.[28] For profound deficiency, treatment is oral dosing with 5 to 20 mg per day. Seizures are reported as resolving in hours to days, with other symptoms resolving within weeks.[27] Treatment of partial biotinidase deficiency is also recommended even though some untreated people never manifest symptoms.[27]

Use in biotechnology

Biotin is widely used throughout the biotechnology industry to conjugate proteins for biochemical assays.[29] Biotin's small size means the biological activity of the protein will most likely be unaffected. This process is called biotinylation. Because both streptavidin and avidin bind strongly to biotin with a dissociation constant Kd in the range of 10−14 to 10−15 M),[30] biotinylated proteins of interest can be isolated from a sample by exploiting this highly stable interaction. The sample is incubated with streptavidin/avidin beads, allowing the capture of the biotinylated protein of interest. Any other proteins binding to the biotinylated molecule will also stay with the bead and all other unbound proteins can be washed away. However, due to the extremely strong streptavidin-biotin interaction, very harsh conditions are needed to elute the biotinylated protein from the beads (typically 6 M guanidine HCl at pH 1.5), which often will denature the protein of interest. To circumvent this problem, beads conjugated to monomeric avidin can be used, which has a decreased biotin-binding affinity of ≈10−8 M, allowing the biotinylated protein of interest to be eluted with excess free biotin.[31]

Interference with medical laboratory results

When people are ingesting high levels of biotin in dietary supplements, a consequence can be clinically significant interference with diagnostic immunoassay blood assays that use biotin-streptavidin technology. This methodology is commonly used to measure levels of hormones such as thyroid hormones, and other analytes such as 25-hydroxyvitamin D. Biotin interference can produce both falsely normal and falsely abnormal results.[1][32] In the US, biotin as a non-prescription dietary supplement is sold in amounts of 1 to 10 mg per serving, with claims for supporting hair and nail health, and as 300 mg per day as a possibly effective treatment for multiple sclerosis[33][34] (see Research). Overconsumption of 5 mg/day or higher causes elevated concentration in plasma that interferes with biotin-streptavidin immunoassays in an unpredictable manner.[24][25] Healthcare professionals are advised to instruct patients to stop taking biotin supplements for 48 h or even up to weeks before the test, depending on the specific test, dose, and frequency of biotin uptake.[24] Guidance for laboratory staff is proposed to detect and manage biotin interference.[25]

History

Further information: Vitamin § History

In 1916, W.G. Bateman observed that a diet high in raw egg whites caused toxic symptoms in dogs, cats, rabbits, and humans.[35] By 1927, scientists such as Margarete Boas and Helen Parsons had performed experiments demonstrating the symptoms associated with "egg-white injury." They had found that rats fed large amounts of egg-white as their only protein source exhibited neurological dysfunction, hair loss, dermatitis, and eventually, death.[36][37]

Hungarian scientist Paul Gyorgy began investigating the factor responsible for egg-white injury in 1933 and in 1939, was successful identifying what he called "Vitamin H" (the H represents Haar und Haut, German for hair and skin).[38][39] Further chemical characterization of vitamin H revealed that it was water-soluble and present in high amounts in the liver.[40] Other research groups, working independently, had isolated the same compound, under different names. In 1936, Kögl and Tönnis isolated a growth factor from egg yolk they called "Bios aus Eigelb."[41] After experiments performed with yeast and Rhizobium trifolii, West and Wilson isolated a compound they called co-enzyme R.[42][43] By 1940, it was recognized that all three compounds were identical and were collectively given the name: biotin.[44] Gyorgy continued his work on biotin and in 1941 published a paper demonstrating that egg-white injury was caused by the binding of biotin by avidin.[45][46]

Using E. coli, a biosynthesis pathway was proposed by Rolfe and Eisenberg in 1968. The initial step was described as a condensation of pimelyl-CoA and alanine to form 7-oxo-8-aminopelargonic acid. From there, they described three-step process, the last being introducing a sulfur atom to form the tetrahydrothiophene ring.[47]

Research

Multiple sclerosis

High-dose biotin (300 mg/day = 10,000 times adequate intake) has been clinical trialed for treatment of multiple sclerosis, a demyelinating autoimmune disease.[33][34] The hypothesis is that biotin may promote remyelination of the myelin sheath of nerve cells, slowing or even reversing neurodegeneration. The proposed mechanisms are that biotin activates acetyl-coA carboxylase, which is a key rate-limiting enzyme during the synthesis of myelin, and by reducing axonal hypoxia through enhanced energy production.[33][34] Clinical trial results are mixed; a 2019 review concluded that a further investigation of the association between multiple sclerosis symptoms and biotin should be undertaken,[33] whereas two 2020 reviews of a larger number of clinical trials reported no consistent evidence for benefits,[48] and some evidence for increased disease activity and higher risk of relapse.[49]

Hair, nails, skin

Biotin is promoted as a dietary supplement for strengthening hair and fingernails, though scientific data supporting these outcomes in humans are very weak.[3][50][51] A review of the fingernails literature reported brittle nail improvement as evidence from two pre-1990 clinical trials that had administered an oral dietary supplement of 2.5 mg/day for several months, without a placebo control comparison group. There is no more recent clinical trial literature.[50] A review of biotin as treatment for hair loss identified case studies of infants and young children with genetic defect biotin deficiency having improved hair growth after supplementation, but went on to report that "there have been no randomized, controlled trials to prove efficacy of supplementation with biotin in normal, healthy individuals."[51] Nevertheless, biotin is marketed as a dietary supplement for nails and hair health. Biotin is also incorporated into topical hair and skin products with similar claims.[52]

Animals

In cattle, biotin is necessary for hoof health. Lameness due to hoof problems is common, with herd prevalence estimated at 10 to 35%. Consequences of lameness include less food consumption, lower milk production, and increased veterinary treatment costs. Dietary supplementation biotin at 20 mg/day reduces the risk of lameness.[53] A review of controlled trials reported that supplementation at 20 mg/day increased milk yield by 4.8%. The discussion speculated that this could be an indirect consequence of improved hoof health or a direct effect on milk production.[54]

For horses, conditions such as chronic laminitis, cracked hooves, or dry, brittle feet incapable of holding shoes are a common problem. Biotin is a popular nutritional supplement. There are recommendations that horses need 15 to 25 mg/day. Studies report biotin improves the growth of new hoof horn rather than improving the status of existing hoof, so months of supplementation are needed for the hoof wall to be completely replaced.[55]

See also

References

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  2. ^ a b c d e f Institute of Medicine (1998). "Biotin". Dietary Reference Intakes for Thiamin, Riboflavin, Niacin, Vitamin B6, Folate, Vitamin B12, Pantothenic Acid, Biotin, and Choline. Washington, DC: The National Academies Press. pp. 374–389. ISBN 0-309-06554-2. Retrieved 2017-08-29.
  3. ^ a b c d e f "Biotin". Micronutrient Information Center, Linus Pauling Institute, Oregon State University, Corvallis, OR. 21 October 2015. Retrieved 16 January 2018.
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  25. ^ a b c Bowen R, Benavides R, Colón-Franco JM, Katzman BM, Muthukumar A, Sadrzadeh H, Straseski J, Klause U, Tran N (December 2019). "Best practices in mitigating the risk of biotin interference with laboratory testing". Clin Biochem. 74: 1–11. doi:10.1016/j.clinbiochem.2019.08.012. PMID 31473202.
  26. ^ a b Wolf B, Grier RE, Secor McVoy JR, Heard GS (1985). "Biotinidase deficiency: a novel vitamin recycling defect". Journal of Inherited Metabolic Disease. 8 (Suppl 1): 53–8. doi:10.1007/BF01800660. PMID 3930841. S2CID 11554577.
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  29. ^ "Overview of Protein Labeling". Thermo Fisher Scientific. Retrieved 22 April 2012.
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  31. ^ Morag E, Bayer EA, Wilchek M (Dec 1996). "Immobilized nitro-avidin and nitro-streptavidin as reusable affinity matrices for application in avidin-biotin technology". Anal Biochem. 243 (2): 257–63. doi:10.1006/abio.1996.0514. PMID 8954558.
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