• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.37-42
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• 1988

In attempts to obtain IMP Producting strains, Brevibacterium ammoniagenes ATCC 6872 was treated wilts N.1.6. Adenine-guanine requiring mutants were obtained from Brevibacterium ammoniagenes ATCC 6872, and then a strain of them was selected for production of IMP and named Brevibacterium ammoniagenes No.9(ade', gu'). The production of IMP by Brevibacterium ammoniagenes nuts No.9 was about 3mg/ml for 4 day of culture. The optimal concentration of adenine and guanine was 150mg/mg.

• The Korean Journal of Food And Nutrition
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• v.6 no.3
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• pp.158-168
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• 1993

For the conversion of WAD to NADP, Immobilized Brevibacterium ammoniagenes cells with NAD kinase was coupled with ATP-generating system by acetate kinase. The membrane permeability of B. ammoniagenes was improved by toluene treatment of cells. The toluene treated B. ammoniagenes cells were immobilized for stable enzyme activity. Partially purified acetate kinase was used in the reaction system. The optimum conditions for the efficient conversion of UAD to WADP by energy-coupled system were investigated. B. ammoniagenes cells treated with toluene for the Improvement of membrane permeability showed 4.5 fold improved permeability in the conversion of NAD to NADP compared with Intact cells. 3% k-carrageenan as the immobilization matrix of B. ammoniagenes showed the best efficiency for the conversion of NAD to NADP The optimum conditions for the WAR to WARP conversion reaction coupled nth ATP-generating system were 10mM acetylphosphate, 5mM ADP 200mM inorganic phosphate, 10mM MgCl2, 250mg/ml Immobilized cells, 49.3mUnit/ml acetate kinase, pH 7.5 and 37$^{\circ}C$. Under the optimum conditions, 72% of 5mM(340mg/ml ) NAD was converted to UADP In 12 hours.

• Microbiology and Biotechnology Letters
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• v.30 no.2
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• pp.105-110
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• 2002

The sequence of 3,221 nucleotides immediately adjacent to rpsA gene encoding 30S ribosomal protein S1 of Brevibacterium ammoniagenes was determined. A putative open reading frame (ORF) of 2,670 nucleotides for a polypeptide of 889 amino acid residues and a TAG stop codon was found, which is located at a distance of 723 nucleotides upstream from rpsA gene with same translational direction. The deduced amino acid sequence of the ORF was found to be highly homologous to the DNA polymerase I of Streptomyces griseus (75.48％), Rhodococcus sp. ATCC 15963 (56.69％), Mycobacterium tuberculosis (55.46％) and Mycobacterium leprae (53.99％). It was suggested that the predicted product of the ORF is a DNA polymerase I with three functional domains. Two domains of 5 → 3 exonuclease and DNA polymerase are highly conserved with other DNA polymerase I, but 3 → 5 exonuclease domain is less conserved.

• Microbiology and Biotechnology Letters
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• v.28 no.3
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• pp.147-151
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• 2000

School of Food Biotechnology, W0050ng University, San 7-6, Jayang~dong. Dong-ku1 Taejon 300-100, Korea - The nucleotide sequence of approximately 2.4 kb immediately adjacent to ptsG gene coding for the glucose permease of Brevibacterium ammoniagenes was detennined. A putative open reading frame (ORP) of 1.467 nucleotides encoding a polypeptide of 489 amino acid residues and a TAA stop codon was identified. The deduced amino acid sequence of the ORF product has a high homology with the 30S ribosomal protein S 1 of Mycohacteriwn tuberculosis (83 % ). M leprae (74%), Streptomyces coelicola (77%), and Escherichia coli (40%). suggesting that the predicted product of ORF is a ribosomal protein S 1. The ORF is located at a distance of 266 nucleotides upstream from ptsC gene with a same translational direction.

• Korean Journal of Microbiology
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• v.22 no.4
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• pp.249-255
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• 1984

To develop the host-vector system for industrial Coryneform bacteria that seemed to be the most suitable microorganisms for molecular breeding of genes involved in the production of amion acids, nucleotides, and other products of industrial interest, broad host range E. coli plasmid R 1162 DNA was transformed into Brevibacterium ammoniagenes and the plasmids pKU6 isolated from a transformant was physically characterized. All other plasmids from the transformed cells except pKU6 exsisted as multimeric forms in Brevibacterium ammoniagenes. The plasmid DNA was retransformed into Corynebacterium glutamicum with a high frequency ($1.32{\times}10^{-1}$ per cell) and maintained stably both in Brevibacterium ammoniagenes and Corynebacterium glutamicum after 100 generations of cultures with 25-30 copy number per cell. The size of both plasmid pKU6 and plasmid R1162 were the same and restriction maps by EcoR I, Ava I, Pst I, Pvu II and Hinc II were also similar.

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.214-221
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• 1998

A Brevibacterium ammoniagenes gene coding for glucose/mannose-specific enzyme II ($EII^{Glc}$) of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was cloned by complementing an Escherichia coli mutation affecting a ptsG gene, and the complete DNA nucleotide sequence was determined. The cloned gene was identified to be a ptsG, which enables the E. coli transportment to use glucose more efficiently than mannose as the sole carbon source in an M9 minimal medium. The ptsG gene of B. ammoniagenes consists of an open reading frame of 1,983 nucleotides putatively encoding a polypeptide of 661 amino acid residues and a TAA stop codon. The deduced amino acid sequence of the B. ammoniagenes $EII^{Glc}$ shows, at $46\%$, the highest degree of sequence similarity with the Corynebacterium glutamicum EII specific for both glucose and mannose. In addition, the $EII^{Glc}$ shares approximately $30\%$ sequence similarities with sucrose-specific and ${\beta}$-glucoside-specific EIIs of the several bacteria belonging to the glucose-PTS class. The 161-amino-acid C-terminal sequence of $EII^{Glc}$ is also similar to that of E. coli enzyme $IIA^{Glc}$, specific for glucose ($EIIA^{Glc}$). The B. ammoniagenes $EII^{Glc}$ consists of three domains; a hydrophobic region (EIIC) and two hydrophilic regions (EIIA, EIIB). The arrangement of structural domains, IIBCA, of the $EII^{Glc}$ is identical to those of EIIs specific for sucrose or ${\beta}$-glucoside. While the domain IIA was removed from the B. ammoniagenes $EII^{Glc}$ the remaining domains IIBC were found to restore the glucose and mannose-utilizing capacity of E. coli mutant lacking $EII^{Glc}$ activity with $EIIA^{Glc}$ of the E. coli mutant. $EII^{Glc}$ contains a histidine residue and a cysteine residue which are putative phosphorylation sites for the protein.

• The Microorganisms and Industry
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• v.26 no.1
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• pp.2-7
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• 2000

Bacterium strain, K-173-10, which was isolated from waste soil of Korean brewing factories, could grow on acetate as the sole carbone source and accumulate a considerable amount of L-glutamic acid (24g/l) in the liguid culture medium. This strain was named by Brevibacterium ammoniagenes sp. by the standard method of taxonomy procedures given in the Manual of Microbiogical Methods.

• Microbiology and Biotechnology Letters
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• v.9 no.1
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• pp.45-50
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• 1981

The effect of growth and the carbon sources including the molar ratio of fructose to glucose was studied for the maximization of inosine-5'-monophosphate (5'-IMP) production from Brebibacterium ammoniagenes D-21530. According to experimental results, fructose was more efficient to 5'-IMP accumulation than glucose, while the latter was better for the cell growth than the former. To synchronously use glucose and fructose as carbon source is to optimally control the cell growth and maximum production of 5'-IMP without change of other conditions. The optimal weight percent of fructose to sum of glucose and fructose was 20～40%, and the productivity improvement over the utilization of fructose was about 40%. And also the optimality of purine base such as adenine and guanine were considered. The optimal concentrations of adenine and guanine were near 50㎎/l.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.04a
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• pp.97.5-98
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• 1978

By the treatment of various mutagens, a number of 5'-guanylic acidproducing from 5'-xanthylic acid were obtained from Brevibacterium ammoniagenes ATCC 6871. The indispensable genetic characters of the mutants were adenine requirement, lack of GMP-reductase and mutation to adenosine resistance from adenosine sensitiveness. Main product of these mutants from 5'-xanthylic acid was 5'-guanylic acid. The substance was isolated in a crystalline form the culture broth of BA 17-2, and identified as 5'-guanylic acid by means of paper chromatography, ultra violet, absorption spectra, and infra red spectrum.

• Korean Journal of Food Science and Technology
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• v.9 no.1
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• pp.1-9
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• 1977

A bacterium strain (K-173-10) which was isolated from waste soil of Korea brewing factory, could be grown on acetate as the sole carbon source and accumulated a considerable amount of L-glutamic acid in the medium. This strain was identified as the new species Brevibacterium ammoniagenes. This study was concerned not only with the culture condition for the production of L-glutamic acid and the cell growth, but also with the effects on concentration of various kind of organic substances, growth factors and penicillin. The results obtained were summarized as follow; 1. It was found that the concentrations of acetate and ammonium ions affected the growth of the bacterium as well as its L-glutamate accumulation. The optimum conditions of the composition of grown media for the growth of the bacterium and its glutamic acid production was found to be 40 g/l of total acetate, $100\;{\mu}g/l$ thiamine, $0.5\;{\mu}g/l$ biotin and $1{\sim}2g/l$ corn steep liquor as the growth factors. 2. Organic acid such as succinic acid, malic acid and ${\alpha}-ketoglutaric$ acid inhibited the cell growth as well as its L-glutamic acid production. 3. The penicillin (20 units/ml) stimulated the production of glutamic acid at appropriate incubation period. 4. It was found that this strain could grow in the presence of urea and ammonium acetate but not in other nitrogen sources.