RIBOFLAVIN

(VITAMIN B2)
By Dahlia Gordon

Forms
Free or protein bound riboflavin is found in milk, eggs,

enriched breads/cereals
Most other foods contain vitamin as a coenzyme
derivative
Flavin mononucleotide (FMN)
Flavin adenine dinucleotide (FAD)

Forms

Daily Requirements
RDA
Male: 1.3 mg
Female: 1.1 mg
Pregnancy: 1.4 mg
Lactation: 1.6 mg
UI
No upper tolerable intake set

Deficiency Disease
Ariboflavinosis
Usually associated with other nutrient deficiencies
Symptoms include: sore throat, redness and swelling of the lining
of the mouth and throat, cracks or sores of the outsides of lips and
at the corners of the mouth, inflammation and redness of the
tongue, and a moist, scaly skin inflammation
Usually does not occur in isolation, usually seen with a combination
of other water soluble vitamin deficiencies

Conditions Related to deficiency

Anemia may develop from severe deficiency
Severe deficiency can diminish the synthesis of Vitamin

B6 and the synthesis of niacin from tryptophan

Deficiency can result in protein and DNA damage
People consuming excess alcohol are at higher risk for
deficiency

Assessment of stores
Measuring the activity of the FAD-dependent enzyme

erythrocyte glutathione reductase

Most precise

Cellular riboflavin concentrations

<10 ug/dL = deficiency
Urinary riboflavin concentrations
<40 ug/g creatine = deficiency

Functions
Acts as an oxidizing agent in many redox reactions
Antioxidant
Xanthine oxidase
FAD-dependent enzyme, catalyzes the oxidation of hypoxanthine and

xanthine to uric acid, which is one of the most effective water-soluble

antioxidants in the blood
glutathione reductase
An FAD-dependent enzyme that participates in the redox cycle of

glutathione
Glutathione peroxidase
Selenium-containing enzymes, require two molecules of reduced

glutathione to break down hydroperoxides

Functions
Energy production
FAD acts as part of the electron transport chain
Helps turn food into ATP
Metabolism of drugs and toxins
Flavocoenzymes work with cytochrome P-450

Availability of nutrient
Light destroys the vitamin
Milk jugs opaque or cardboard cartons
Vitamin is fairly resistant to heat, oxidation, and acid

Food Sources
Animal origins, mostly milk and milk products
3 oz. liver = 2-3 mg
1 cup plain nonfat yogurt = 0.48 mg
1 cup nonfat milk = 0.45 mg
One egg = 0.26 mg
3 oz. meat = 0.1-0.25 mg
1 oz cheese = 0.08-0.11mg
cup legumes = 0.05 mg
Fortified breads and cereals also contain riboflavin

Absorption
Most riboflavin in food is present as the derivative FAD and FMN
a prerequisite for the absorption of dietary riboflavin is the hydrolysis

of FAD and FMN to riboflavin

process is accomplished by the action of hydrochloric acid secreted within the

stomach and by gastric and intestinal enzymatic hydrolysis of the protein

this is catalyzed by nonspecific phosphatases in the brush border membranes of
enterocytes

Absorption takes place mostly in the small intestine through an active,

carrier-mediated, saturable transport process

When large amounts of the vitamin are digested, riboflavin may be
absorbed by diffusion, the presence of bile facilitates this
Carrier mediated absorption can also occur in the colon where
riboflavin is synthesized by bacterial metabolism
Absorption of riboflavin is increased when taken with other B Vitamins
and Vitamin C

Transport
Carried to the liver where it is converted again to FMN by

flavokinase and to its other predominant flavoenzyme in

tissues, FAD, by FAD synthetase
FAD, FMN, and riboflavin are transported in the plasma
bound membrane by both albumin and certain
immunoglobulins, which also bind to flavin coenzymes
Albumin is the main transport protein

Storage and Metabolism

Riboflavin is found in small quantities in a variety of

tissues
Greatest concentrations are in the heart, liver, and kidney

Within cells, when riboflavin is converted to its coenzyme

forms by flavokinase and FAD synthetase both are widely

distributed in tissues in the liver, spleen, small intestine,
kidneys and heart
FMN is the major form present in cells
(about 60-95%)

FAD follows
(about 5-20%)

Metabolism
Synthesis of FMN and FAD are influenced by end product

inhibition and hormones including ACTH

(adrenocorticotropic hormone), aldosterone, and the
thyroid hormones
Almost all riboflavin in tissues is enzyme bound, unbound
flavins are rapidly hydrolyzed to free riboflavin, which
diffuses from cells and is excreted
The intracellular phosphorylation of riboflavin is therefore
a form of metabolic trapping key to riboflavin homeostasis

Excretion
Most riboflavin is excreted by urine
About 60-70%
Only small amounts of riboflavin are lost in feces
Fecal riboflavin metabolites come from the catabolism of riboflavin
by intestinal bacteria

Prevention of diseases and conditions

Cataracts
Early evidence shows that riboflavin might help prevent cataracts
In a double-blind, placebo-controlled study people took a niacin
and riboflavin supplement and had fewer cataracts than people
who took other vitamins
Research couldnt show if niacin or riboflavin caused this
Migraines
One study showed that taking 400 mg of riboflavin/day cut the

number of migraine attacks in half

Memory loss
Memory may be improved by these supplements, according to
some research done on older people
People with higher riboflavin levels scored higher on memory tests

Nutrigenomics
Riboflavin (1.6mg) was given to hypertensive individuals
Individuals with the MTHFR677TT genotype saw a

decrease in blood pressure that was more effective than

current antihypertensive drugs
Indicates the potential for a personalized approach to the
management of hypertension in this genetically at-risk
group

Public Health
a randomized trial of adding an iron- and riboflavin-rich

powder to school meals in India

Reduced anemia in five to nine year old children by more than fifty

percent
Also essentially eliminated clinical signs of riboflavin deficiency

Supplement Recommendations
Most Americans get enough riboflavin from a balanced

diet
Could be taken for:
Treatment of low levels of riboflavin
Preventing migraine headaches (400 mg)
Preventing cataracts (2.6 mg + 40 mg niacin)

Works Cited

Turner J. Riboflavin. The Gale Encyclopedia of Nursing and Allied Health. 2013:2940-2942
McDowell LR. Riboflavin. In: Ames, Iowa, USA: Iowa State University Press:311-346.
Advanced Nutrition and Human Metabolism, 6th Edition, Gropper, S. and Smith, J. eds.
Wadsworth, Belmont CA, 2013.
Wilson CP, McNulty H, Ward M, et al. Blood Pressure in Treated Hypertensive Individuals With
the MTHFR 677TT Genotype Is Responsive to Intervention With Riboflavin: Findings of a
Targeted Randomized Trial. Hypertension. 2013;61:1302-1308
McNulty H, Strain J, Ward M. Riboflavin lowers blood pressure in hypertensive people with the
MTHFR 677TT genotype. Archives of public health = Archives belges de sant publique.
2014;72:K2-K2.
Higdon, J. Micronutrient Information Center: Riboflavin. Linus Pauling Institute, Micronutrient
Research for Optimal Health. September 2002. Available at:
http://lpi.oregonstate.edu/infocenter/vitamins/riboflavin/. Accessed February 2015.
Ehrlich, S. Vitamin B2 (Riboflavin). University of Maryland Medical Center website. June 2011.
Available at: http://umm.edu/health/medical/altmed/supplement/vitamin-b2-riboflavin. Accessed
February 2015.
Vinodkumar M, Rajagopalan S. Efficacy of fortification of school meals with ferrous glycine
phosphate and riboflavin against anemia and angular stomatitis in schoolchildren. Food and
nutrition bulletin. 2009;30:260
Bowers HJ. Riboflavin (vitamin B-2) and health. Am J Clin Nutr. 2003;77:1352