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  Minerals
Boron

Calcium

Chromium

Cobalt

Copper

Fluoride

Iodine

Iron

Magnesium

Manganese

Molybdenum

Potassium

Selenium

Zinc

Biotin

Red Arrow  Facts Red Arrow  Functions
Red Arrow  Deficiency signs and symptoms Red Arrow  Toxicity
Red Arrow  Dietary Sources Red Arrow  Populations w/ Special Needs
Red Arrow  Requirements & Recommendations Red Arrow  Drug-Vitamin Interaction
Red Arrow  Research Summary

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 Facts Topic header down arrow
  • Biotin is one of the B vitamins. It is a water-soluble and sulfur-containing vitamin.
  • Biotin is necessary for the production and utilization of fats and amino acids in the body.
  • Mammals and many species of plants are unable to synthesize biotin; however, biotin is synthesized by bacteria, yeast, other fungi and algae, and by certain plant species.
  • Because bacteria synthesize biotin, the microflora of the large intestine contributes to the human body’s biotin requirements.
  • The amount of biotin found in foods is much lower when compared to other B vitamins.
  • Avidin found in raw egg white binds tightly to biotin, resulting in a decreased absorption. However, cooking inactivates avidin.
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 Functions Topic header down arrow
  • Biotin is a cofactor for enzymes that are involved in the metabolism of carbohydrate, fat, and protein. Enzymatic reactions involving biotin allow the transfer of carbon dioxide, CO2, in biochemical reactions that are essential for the metabolism of carbohydrates, fat, and protein.
  • As a coenzyme, biotin plays a role in the deamination, which generates energy from certain amino acids.
  • The four carboxylase enzymes in mammalian tissue that require biotin are: acetyl coenzyme A (CoA) carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and â-methylcrotonyl CoA carboxylase.
  • Biotin is involved in the formation of purines, an essential part of DNA and RNA.
  • Biotin may modulate gene expression at the transcriptonal and translational concentrations.
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 Deficiency signs and symptoms Topic header down arrow
  • Although clinical deficiency of biotin is rare, it can occur from prolonged consumption of raw egg whites, which contains the biotin-binding protein, avidin. Avidin is destroyed by cooking. Deficiency can also occur from long-term total parenteral nutrition, a genetic defect in the biotin-dependent enzymes, or from malabsorption syndromes such as short-gut syndrome.
  • Some signs of biotin deficiency are:
    • dry, scaly skin
    • nausea
    • anorexia
    • seborrheic dermatitis
    • alopecia (hair loss)
    • conjunctivitis
    • neurological abnormalities
Note: These symptoms are also common to a deficiency in essential fatty acids.
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 Toxicity Topic header down arrow
No toxic effects of oral biotin have been reported in humans or animals, even at doses up to 10 mg/day. Biotin is found in multivitamin/mineral supplements which typically contain between 30 – 60 mcgs per daily dose.
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 Dietary Sources Topic header down arrow
Biotin is widely distributed throughout the food supply, but some of the more concentrated sources of biotin include:
egg yolksoybeans
organ meats(i.e. liver, kidney)
yeastcheese
barleybrewers yeast
milk
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 Populations w/ Special Needs Topic header down arrow
Individuals with a carboxylase deficiency are usually treated with pharmacologic doses of biotin. A study showed that high oral doses of biotin were completely absorbed in healthy adults. 2
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 Requirements & Recommendations Topic header down arrow
Biotin: Dietary Reference Intake 1:
(mcg/day)*
Infants
0 to 6 months
7 to 12 months
5
6
Children
1-3 years
4-8 years
8
12
Males:
9-13 years
14-18 years
19+ years
20
25
30
Females:
9-13 years
14-18 years
19+ years
20
25
30
Pregnancy:
<=18 years
19-50 years
30
30
Lactation:
<=18 years
19-50 years
35
35


* Values are Adequate Intakes (AI). Tolerable Upper Intake levels (UL) are not determinable due to lack of data of adverse effects.
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 Drug-Vitamin Interaction Topic header down arrow
Anticonvulsants, such as carbamazepine and Phenobarbital, may deplete biotin by competing with it for absorption in the intestine. Biotin supplementation may be helpful during long-term anticonvulsant therapy. Also, taking biotin supplements two to three hours apart from the drug prevents this potential interaction.

Information on the relationship between substances and disease is provided for general information, in order to convey a balanced review of the scientific literature. In many cases the relationship between a substance and a disease is tentative and additional research is needed to confirm such a relationship. 3 4 5
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 Research Summary Topic header down arrow
Nutrient Interaction: Biotin and lipoic acid have structural similarities. Rats were treated with different doses of lipoic acid with or without biotin for 28 days and hepatic enzyme activities were measured. As a result, activities of pyruvate carboxylase and â-methylcrotonyl-CoA were lowered by lipoic acid, but not by lipoic acid plus biotin. Since lipoic acid has gained popularity as a dietary supplement to treat diabetic neuropathy, caution should be taken. 6

Cytokine Release: Biotin was found to have a role in regulating the genetic expression of biotin-dependent carboxylase at the mRNA concentration in rats in a study. The results suggested that biotin acts as a modulator in the genetic expression of the enzymes involved in its function as a cofactor (i.e. holocarboxylase synthetase). 7 Another study investigated the effects of a pharmacological dose of biotin on cell proliferation in peripheral blood mononuclear cells (PBMC) and cytokine release in healthy adults. Healthy adults were given ~750 mcg/day of biotin for 14 days. Results showed that the pharmacological dose of biotin did not change the percentage of PBMC, but decreased synthesis of interleukin-1ß and interleukin-2. 8
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