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L-Glutamic acid

MSG, C8H8NNa04,H20. Flavouring agent extensively used as a food additive. Prepared from natural or synthetic L-glutamic acid. [Pg.364]

Ammonia reacts with the ketone carbonyl group to give an mine (C=NH) which is then reduced to the amine function of the a ammo acid Both mine formation and reduc tion are enzyme catalyzed The reduced form of nicotinamide adenine diphosphonu cleotide (NADPH) is a coenzyme and acts as a reducing agent The step m which the mine is reduced is the one m which the chirality center is introduced and gives only L glutamic acid... [Pg.1124]

L Glutamic acid is not an essential ammo acid It need not be present m the diet because animals can biosynthesize it from sources of a ketoglutaric acid It is however a key intermediate m the biosynthesis of other ammo acids by a process known as transamination L Alanine for example is formed from pyruvic acid by transamination from L glutamic acid... [Pg.1124]

In transamination an amine group is transferred from L glutamic acid to pyruvic acid An outline of the mechanism of transamination is presented m Figure 27 4... [Pg.1124]

Crystalline Structures. Crystal shape of amino acids varies widely, for example, monoclinic prisms in glycine and orthorhombic needles in L-alanine. X-ray crystallographic analyses of 23 amino acids have been described (31). L-Glutamic acid crystallizes in two polymorphic forms (a and P) (32), and the a-form is mote facdely handled in industrial processes. The crystal stmeture has been determined (33) and is shown in Figure 1. [Pg.274]

Manometric determiaation of L-lysiae, L-argioine, L-leuciae, L-ornithine, L-tyrosiae, L-histidine, L-glutamic acid, and L-aspartic acid has been reviewed (136). This method depends on the measurement of the carbon dioxide released by the T.-amino acid decarboxylase which is specific to each amino acid. [Pg.285]

In the 1950s, a group of coryneform bacteria which accumulate a large amount of L-glutamic acid in the culture medium were isolated (21). The use of mutant derivatives of these bacteria offered a new fermentation process for the production of many other kinds of amino acids (22). The amino acids which are produced by this method are mostiy of the T.-form, and the desired amino acid is singly accumulated. Therefore, it is very easy to isolate it from the culture broth. Rapid development of fermentative production and en2ymatic production have contributed to the lower costs of many protein amino acids and to their availabiUty in many fields as economical raw materials. [Pg.285]

L-Glutamic acid "glutamic acid bacteria" such as Corymb, glutamicum Brerib. Jlavum Brevib. lactojermentum Microb. ammoniaphilum wild penicillin is added, or biotm is limited >100, 50% 21... [Pg.287]

L-glutamic acid C. melassecola C. melassecola Glu A, citrate dehydrogenase, ppc, aconitate dehydratase ... [Pg.290]

An estimation of the amount of amino acid production and the production methods are shown ia Table 11. About 340,000 t/yr of L-glutamic acid, principally as its monosodium salt, are manufactured ia the world, about 85% ia the Asian area. The demand for DL-methionine and L-lysiae as feed supplements varies considerably depending on such factors as the soybean harvest ia the United States and the anchovy catch ia Pern. Because of the actions of D-amiao acid oxidase and i.-amino acid transamiaase ia the animal body (156), the D-form of methionine is as equally nutritive as the L-form, so that DL-methionine which is iaexpensively produced by chemical synthesis is primarily used as a feed supplement. In the United States the methionine hydroxy analogue is partially used ia place of methionine. The consumption of L-lysiae has iacreased ia recent years. The world consumption tripled from 35,000 t ia 1982 to 100,000 t ia 1987 (214). Current world consumption of L-tryptophan and i.-threonine are several tens to hundreds of tons. The demand for L-phenylalanine as the raw material for the synthesis of aspartame has been increasing markedly. [Pg.291]

D-glutamic acid L-glutamic acid Glu decarboxylase + Glu racemase iMctohac. brevis 207... [Pg.293]

In Foods. Each amino acid has its characteristic taste of sweetness, sourness, saltiness, bitterness, or "umami" as shown in Table 13. Umami taste, which is typically represented by L-glutamic acid salt (and some 5 -nucleotide salts), makes food more palatable and is recognized as a basic taste, independent of the four other classical basic tastes of sweet, sour, salty, and bitter (221). [Pg.296]

In Industrial Chemicals. Recendy, as some amino acids (eg, L-glutamic acid, L-lysine, glycine, DL-alanine, DL-methionine) have become less expensive chemical materials, they have been employed in various appHcation fields. Poly(amino acid)s are attracting attention as biodegradable polymers in connection with environmental protection (236). [Pg.297]

The a-carbon of glutamic acid is chiral. A convenient and effective means to determine the chemical purity of MSG is measurement of its specific rotation. The specific optical rotation of a solution of 10 g MSG in 100 mL of 2 A/HQ is +25.16. Besides L-glutamic acid [56-86-0] D-glutamic acid [6893-26-1] and the racemic mixture, DL-glutamic acid [617-65-2] are known. Unique taste modifying characteristics are possessed only by the L-form. [Pg.303]

L-Glutamic acid does not racemize in neutral solution, even at 100°C. Deviation of pH from neutral to greater than 8.5 results in thermal racemization with loss of taste characteristics. Racemization in neutral solution occurs at 190 °C after formation of the lactam, 5-oxo-L-proline, pyroglutamic acid [98-79-3]. [Pg.303]

The reaction is very slow in neutral solution, but the equiUbrium shifts toward the lactam rather than glutamic acid. Under strongly acidic or alkaline conditions, the ring-opening reaction requires a very short time (10). Therefore, neutralization of L-glutamic acid should be performed cautiously because intramolecular dehydration is noticeable even below 190°C. [Pg.303]

Glutamic acid dehydrogenase is widely distributed in microorganisms and higher plants as a catalyst in the synthesis of L-glutamic acid from a-ketoglutaric acid and free ammonia. Transaminase is contained in a wide variety of microorganisms. [Pg.303]


See other pages where L-Glutamic acid is mentioned: [Pg.1124]    [Pg.1124]    [Pg.558]    [Pg.875]    [Pg.446]    [Pg.446]    [Pg.446]    [Pg.446]    [Pg.446]    [Pg.446]    [Pg.446]    [Pg.146]    [Pg.441]    [Pg.476]    [Pg.271]    [Pg.272]    [Pg.272]    [Pg.274]    [Pg.282]    [Pg.283]    [Pg.285]    [Pg.285]    [Pg.285]    [Pg.286]    [Pg.287]    [Pg.287]    [Pg.289]    [Pg.289]    [Pg.291]    [Pg.293]    [Pg.303]    [Pg.303]   
See also in sourсe #XX -- [ Pg.1112 , Pg.1114 , Pg.1119 , Pg.1123 , Pg.1124 ]




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Amino acids L-glutamate

Azobenzene-containing Poly(L-glutamic acid)

BOC-L-Glutamic acid

Formimino-L-glutamic acid

Glutamic acid/glutamate

Glycyl-L-glutamic acid

L-Glutamate

L-Glutamic Acid Hydrochloride

L-Glutamic acid decarboxylase

L-Glutamic acid dehydrogenase

L-Glutamic acid derivatives

L-Glutamic acid diethyl ester

Of L-glutamic acid

Poly-L-glutamic acid

Poly-L-glutamic acid conjugates

Poly-a,L-glutamic acid

Y- -L-glutamic acid

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