Beruflich Dokumente
Kultur Dokumente
On
RIBOFLAVIN
And
THIAMINE
Riboflavin, also known as vitamin B2 is an easily absorbed colored micronutrient with a key role in
maintaining health in humans and animals. Vitamin B2 is required for a wide variety of cellular processes.
The name "riboflavin" comes from "ribose" (the sugar whose reduced form, ribitol, forms part of its
structure) and "flavin", the ring-moiety which imparts the yellow color to the oxidized molecule (from
Latin flavus, "yellow"). The reduced form, which occurs in metabolism along with the oxidized form, is
colorless. The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules
of ribulose 5-phosphate.
CHEMICAL PROPERTIES:
a.
b.
c.
d.
e.
RIBOFLAVIN
BIOCHEMICAL FUNCTIONS:
a. It plays a key role in energy metabolism, metabolism of fats, ketone bodies, carbohydrates, and
proteins.
b. It is the central component of the cofactors FAD (Flavin adenine dinucleotide) and FMN (Flavin
mononucleotide), and is therefore required by all flavoproteins.
c. FMN and FAD function as coenzymes for a wide variety of oxidative enzymes and remain bound
to the enzymes during the oxidation-reduction reactions.
d. Flavins can act as oxidizing agents because of their ability to accept a pair of hydrogen atoms.
Reduction of isoalloxazine ring (FAD, FMN oxidized form) yields the reduced forms of the
flavoproteins (FMNH2 and FADH2).
e. Riboflavin is also needed to help the body change vitamin B 6 and folate into forms it can use.
f. It is also important for body growth and red blood cell production.
OTHER USES:
a. Riboflavin is yellow or yellow-orange in color and in addition to being used as a food coloring; it
is also used to fortify some foods.
b. It is used in baby foods, breakfast cereals, pastas, sauces, processed cheese, fruit drinks, vitaminenriched milk products, and some energy drinks.
c. As riboflavin is fluorescent under UV light, dilute solutions (0.015-0.025% w/w) are often used
to detect leaks in an industrial system such a chemical blend tank or bioreactor.
d. Riboflavin has been used in several clinical and therapeutic situations. Riboflavin supplements
have been used as part of the phototherapy treatment of neonatal jaundice.
e. Riboflavin and UV light treatment has been shown to be effective for inactivating pathogens in
platelets and plasma, and is under development for application to whole blood.
SOURCES:
Milk, cheese, leaf vegetables, liver, kidneys, legumes, yeast, mushrooms, milk, yogurt, meat, eggs, fish,
green beans and almonds are good sources of vitamin B2, but exposure to light destroys riboflavin.
Cereals grains contain relatively low concentrations of flavins, but are important sources in those parts of
the world where cereals constitute the staple diet. The milling of cereals results in considerable loss (up to
60%) of vitamin B2. Free riboflavin is naturally present in foods along with protein-bound FMN and
FAD. Bovine milk contains mainly free riboflavin, with a minor contribution from FMN and FAD. In
whole milk, 14% of the flavins are bound noncovalently to specific proteins. Egg white and egg yolk
contain specialized riboflavin-binding proteins, which are required for storage of free riboflavin in the egg
for use by the developing embryo.
DEFICIENCY SYMPTOMS:
THIAMINE
THIAMINE
b. Thiamine diphosphate: ThDP is a coenzyme for several enzymes that catalyze the transfer of twocarbon units and in particular the dehydrogenation (decarboxylation and subsequent conjugation
with coenzyme A) of 2-oxoacids (alpha-keto acids).
c. Thiamine triphosphate: Thiamine triphosphate (ThTP) is considered as a specific neuroactive
form of thiamine.
d. Adenosine thiamine triphosphate
e. Adenosine thiamine diphosphate
BIOSYNTHESIS:
Complex thiamine biosynthetic pathways occur in bacteria, some protozoans, plants and fungi. The
thiazole and pyrimidine moieties are synthesized separately and then assembled to form ThMP by
thiamine-phosphate synthase. In most bacteria and in eukaryotes, ThMP is hydrolyzed to thiamine, that
may then be pyrophosphorylated to ThDP by thiamine diphosphokinase. The biosynthetic pathways are
regulated by riboswitches in all organisms that synthesize thiamine.
OCCURANCE IN FOOD:
Thiamine is found in a wide variety of foods at low concentrations. Yeast, yeast extract, and pork are the
most highly concentrated sources of thiamine. In general, cereal grains are the most important dietary
sources of thiamine.
DEFICIENCY SYMPTOMS:
a. Thiamine deficiency has a potentially fatal outcome if it remains untreated.
b. In less severe cases, nonspecific signs include malaise, weight loss, irritability and confusion.
c. Thiamine derivatives and thiamine-dependent enzymes are present in all cells of the body, thus a
thiamine deficiency would seem to adversely affect all of the organ systems. However, the
nervous system is particularly sensitive to thiamine deficiency, because of its dependence on
oxidative metabolism.
d. Thiamine deficiency commonly presents subacutely and can lead to metabolic coma and death.
e. A lack of thiamine can be caused by malnutrition, a diet high in thiaminase-rich foods (raw
freshwater fish, raw shellfish, ferns) and foods high in anti-thiamine factors (tea,coffee, betel
nuts) and by grossly impaired nutritional status associated with chronic diseases, such as
alcoholism, gastrointestinal diseases, HIV-AIDS, and persistent vomiting.
f.
Well-known syndromes caused by thiamine deficiency include beriberi, Wernicke-Korsakoff
syndrome and optic neuropathy.