Brevibacterium flavum

Auxotrophic mutants are used in the production of end products of branched pathways, ie pathways leading to more than one amino add at the same time. This is the case for L-lysine, L-methicmine, L-threonine and L-isoleudne in Brevibacterium flavum and Corynebacterium glutamicum. 

Amino acids, e.g. glutamate, lysine Corynebacterium glutamicum Brevibacterium flavum Supplementation of feeds/food intravenous infusion fluid constituents... 

Lysine, threonine Corynebacterium glutamicum, Brevibacterium flavum, Escherichia coli Essential amino-acids, added to supplement low grade protein... 

I Takata, K Kayashima, T Tosa, I Chibata. Improvement of stability of fumarase activity of Brevibacterium flavum by immobilization with A>carrageenan. J Ferment Technol 60 431-437, 1982. 

A fermentation process for producing lysine was made possible by using mutants of Corynebacterium glutamicum or Brevibacterium flavum. Both auxotrophic and regulatory mutants have been obtained for overproduction of lysine. Figure 30.19 shows the biosynthetic... 

Among the amino acids, L-glutamic acid can enhance or improve the flavor of foods. Glutamic acid is produced via fermentation directly from sugar using organisms such as Corvnebacterium glutamicum and Brevibacterium flavum.(66). 

Efforts to develop organisms that overproduce L-phenylalanine have been vigorously pursued by the Nutrasweet Company, Ajinomoto, Kyowa Hakko Kogyo, and others. The focus has centered on bacterial strains that have previously demonstrated the ability to overproduce other amino acids. Such organisms include principally the coryneform bacteria, Brevibacterium flavum [1,2] and Corynebac-terium glutamicum [3,4] used in L-glutamic acid production. In addition, Escherichia coli has been extensively studied for L-phenylalanine manufacture due to... 

A biocatalytic enantioselective addition of ammonia to a C=C bond of an afl-unsaturated compound, namely fumaric acid, makes the manufacture of L-aspar-tic acid, l-27, possible [30], This L-amino acid represents an important intermediate for the production of the artificial sweetener aspartame. The biocatalytic production process, which is applied on an industrial scale by, e.g., Kyowa Hakko Ko-gyo and Tanabe Seiyaku, is based on the use of an aspartate ammonia lyase [E.C.4.3.1.1] [31]. As a biocatalyst, an immobilized L-aspartate ammonia lyase from Escherichia coli [32, 33] as well as Brevibacterium flavum whole-cell catalysts [32 a, 34] have been applied successfully. 

The analogous biocatalytic process using whole-cells from Brevibacterium flavum also led to L-aspartic acid, l-27, in high yields of >99%, and excellent enantioselectivities of >99% ee [33], This process that is carried out under basic conditions at pH 9-10 has been developed by Mitsubishi Petrochemical. 

The combined utilization in a single reactor of both aspartase from Brevibacterium flavum and aspartate-P-decarboxylase from Pseudomonas dacunhae, thereby catalyzing the reaction from fumaric acid via L-aspartic acid to L-alanine (5), has also been developed by Mitsubishi 5. ... 

Three immobilized enzyme or microbial cell systems currently used industrially in synthesis of chiral amino acids plus one presently under development are described. L-amino acids are produced by enzymatic hydrolysis of DL-acylamino acid with aminoacylase immobilized by ionic binding to DEAE-Sephadex. Escherichia coli cells immobilized by K-carrageenan crosslinked with glutaraldehyde and hexamethylenediamine are used to convert fumaric acid and cimmonia to L-aspartic acid and Brevibacterium flavum cells similarly immobilized are used to hydrate fumaric acid to L-malic acid. The decarboxylation of L-aspcirtic acid by immobilized Pseudomonas dacunhae to L-alanine is currently under investigation. 

COMPARISON OF PRODUCTIVITIES OF Brevibacterium ammoniagenes AND Brevibacterium flavum IMMOBILIZED WITH POLYACRYLAMIDE AND WITH CARRAGEENAN FOR PRODUCTION OF L-MALIC ACID... 

The behavior of invertebrate and plant GDH s has been less extensively studied than that of the bovine enzyme. The question of compulsory order as opposed to random order binding, which has been resolved only with great difficulty for bovine GDH, has been investigated with only a few other GDH s. In each case, for Phycomycetes GDH (NAD) (S3S), GDH (NADP) of Brevibacterium flavum 30), soybean GDH (NAD), 7), and both the NAD- and NADP-dependent GDH s of Thio-bacillus novellm (33), compulsory order binding has been reported in which coenzyme binds first and NH4+ last. However, since the more refined methods employed for investigation of the mechanism of bovine GDH have not been applied to any of these systems, the question of random vs. ordered mechanism cannot be said to have been resolved, particularly since the methods thus far employed did not give decisive results with bovine GDH. 

Production of L-isoleucine from ethanol and a-keto butyric acid or a-amino butyric acid using a multistep bioconversion with Brevibacterium flavum under native immobilization and biotin-free conditions (Mitsubishi Petrochemical Co., Inc.). Productivity of this system is 200 mmol 1-1 d "1. 

Miyajima, R. Shiio, I. Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. V. Properties of homoserine kinase. J. Bio-chem., 71, 219-226 (1972)... 

Brevibacterium ammoniagenes cells immobilized by copolymerization with acrylamide have been used in column form for the continuous production in high yield of pure nicotinamide adenine dinucleotide phosphate, for the continuous production of L-malic acid from fumaric acid, and for study of the NAD-kinase activity of the immobilized cells. The continuous production of L-malic acid has also been achieved with Brevibacterium flavum cells immobilized by gelation in k-carrageenan. ... 

L-Malate (from fumarate) Gibberellic acid (from cheese whey) 2,3-Butanediol (from whey permeate) L-Glutamic add Fumarase Brevibacterium ammonia genes Fusarium moniUform cells Klebsiella pneumoniae cells Brevibacterium flavum (multienzyme)... 

I. (1965) Comparative studies on the mechanism of microbial glutamate formation. I. Pathway of glutamate formation from glucose in Brevibacterium flavum and in Micrococcus glutami-cus. J. Gen. Appl. Microbiol, 11 (4), 285-294. 

Shiio, I., Otsuka, S., and Tsunoda, T. (1959) Glutamic add formation from glucose by bacteria. II. Glutamic acid and a-ketoglutaric add formation by Brevibacterium flavum No. 2247. /. Biochem., 46 (12), 1597-1605. 

Ozaki, H. and Shiio, I. (1969) Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. 

Regulation of glucose-6-phosphate dehydrogenase in Brevibacterium flavum. Agric. Biol. Chem., 51 (1),... 

Sugimoto, S., Nakagawa, M., Tsuchida, T., and Shiio, I. (1973) Regulation of aromatic amino acid biosynthesis and production of tyrosine and phenylalanine in Brevibacterium flavum. Agric. Biol Chem., 37 (10), 2327-2336. 

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