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Riboflavin, also known as vitamin B 2, is a vitamin found in food and sold as a dietary supplement. [3] It is essential to the formation of two major coenzymes, flavin mononucleotide and flavin adenine dinucleotide. These coenzymes are involved in energy metabolism, cellular respiration, and antibody production, as well as normal growth and ...
The most common organism used for production of riboflavin through fermentation is Eremothecium ashbyii. Once riboflavin is produced it must be extracted from the broth, this is done by heating the cells for a certain amount of time, and then the cells can be filtered out of solution. Riboflavin is later purified and released as final product. [3]
It is a colorless solid. It is a precursor for the production of riboflavin (vitamin B 2). [1] The compound is prepared by two routes: hydrogenation of (2-chloromethyl)-4-nitrotoluene and reaction of the bromoxylene with ammonia. [1]
In 2008, the global need for riboflavin was 6,000 tons per year, with production capacity of 10,000 tons. [4] This $150 to 500 million market is not only for medical applications, but is also used as a supplement to animal food in the agricultural industry and as a food colorant .
Riboflavin synthase is an enzyme that catalyzes the final reaction of riboflavin biosynthesis. It catalyzes the transfer of a four-carbon unit from one molecule of 6,7-dimethyl-8-ribityllumazine onto another, resulting in the synthesis of riboflavin and 5-amino-6-ribitylamino-2,4(1 H ,3 H )-pyrimidinedione :
Vitamin B 2 (Riboflavin) Meat, dairy products, eggs: 1922: Vitamin E (Tocopherol) Wheat germ oil, unrefined vegetable oils 1929: Vitamin K 1 (Phylloquinone) Leaf vegetables: 1931: Vitamin B 5 (Pantothenic acid) Meat, whole grains, in many foods 1934: Vitamin B 6 (Pyridoxine) Meat, dairy products 1936: Vitamin B 7 [26] Meat, dairy products, Eggs ...
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B 2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. [1]
Its structure was determined and reported in 1935 and given the name riboflavin, derived from the ribityl side chain and yellow colour of the conjugated ring system. [ 6 ] The first evidence for the requirement of flavin as an enzyme cofactor came in 1935.