• Journal of the Korea Organic Resources Recycling Association
• /
• v.6 no.1
• /
• pp.13-20
• /
• 1998

Rhodospirillum rubrum N-1 was inoculated to manipulated swine wastewater of 20,000 mg/L as Biochemical Oxygen Demand (BOD) to study the effect of aeration on swine wastewater deodorization. Biological and physico-chemical parameters were determined at 1 day interval for 9 days. Removals of BOD, volatile fatty acids (VFAs), and phosphate were 54.6%, 87.0%, and 54.5%, respectively. No significant changes were observed in the concentrations of total nitrogen, total phosphorus, nitrate, nitrite, hydrogen sulfide, and mercaptane.

• Journal of Microbiology
• /
• v.39 no.3
• /
• pp.168-176
• /
• 2001

Five different types of catalases from photosynthetic bacterium Rhodospirillum rubrum S1 grown aerobically in the dark were found in this study, and designated Catl (350 kDa), Cat2 (323 kDa), Cat3 (266 kDa), Cat4 (246 kDa), and Cat5 (238 kDa). Analysis of native PAGE revealed that Cat2, Cat3, and Cat4 were also produced in the cells anaerobically grown in the light. It is notable that only Cat2 was expressed much more strongly in response to the anaerobic condition. Enzyme activity staining demonstrated that Cat3 and Cat4 had bifunctional catalase-peroxidase activities, while Catl, Cat2, and Cat5 were typical monofunctional catalases. S1 cells grown aerobically in the presence of malate as the sole source of carbon exhibited an apparent catalase Km value of 10 mM and a Vmax of about 705 U/mg protein at late stationary growth phase. The catalase activity of Sl cells grown in the anaerobic environment exhibited a much lower Vmax of about 109 U/mg protein at late logarithmic growth phase. The catalytic activity was stable in the broad range of temperatures (30$\^{C}$-60$\^{C}$), and pH (6.0-10.0). R. rubrum S1 was much more resistant to H$_2$O$_2$in the stationary growth phase than in the exponential growth phase regardless of growth conditions. Cells of stationary growth phase treated with 15 mM H$_2$O$_2$for 1 h showed 3-fold higher catalase activities than the untreated cells. In addition, L-glutamate induced an 80-fold increase in total catalase activity of R. rubrum S1 compared with magic acid. Through fraction analyses of S1 cells, Cat2, Cat3, Cat4 and Cat5 were found in both cytoplasm and periplasm, while Catl was localized only in the cytoplasm.

• Applied Biological Chemistry
• /
• v.36 no.6
• /
• pp.488-494
• /
• 1993

A photosynthetic bacterium strain P17 having high growth rate and assimilating ability of organic acids was isolated from several soil samples, which was identified as Rhodospirillum rubrum. Cultural conditions of the strain P17 were examined for the production of starter culture used in the treatment of organic waste water. The addition of organic acids mixture as carbon source containing 0.2% Na-acetate, 0.1% Na-propionate and 0.2% Na-lactate and 0.1% of yeast extract as growth factor stimulated the cell growth. The maximal cell production was obtained at $30^{\circ}C$, pH 7.0, 2,500 lux of illumination and $50{\sim}100\;rpm$ of agitation. Under the optimal conditions of batch and fed-batch culture systems in a Jar fermentor, 5.17 g/l and 7.93 g/l of cells were obtained after S days of cultivation, respectively. In continuous culture system, the cell productivity was 0.206 g/l/h at a dilution rate of 0.21 $h^{-1}$. When R. rubrum P17 was cultivated in a soybean curd waste water, initial COD level(3,240 mg/l) of the waste water was reduced to 250 mg/l after 4 days of cultivation.

• Journal of Microbiology
• /
• v.44 no.2
• /
• pp.185-191
• /
• 2006

The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH $(5.0{\sim}9.0)$, and remained stable over a broad temperature range $(20^{\circ}C{\sim}60^{\circ}C)$. It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19 % of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50 % at concentrations of $11.5{\mu}M,\;0.52{\mu}M,\;and\;0.11{\mu}M$, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase.

• Journal of the Korea Organic Resources Recycling Association
• /
• v.5 no.1
• /
• pp.25-32
• /
• 1997

The effect of levulinic acid (LA) and biosynthetic precursors of ${\delta}$-aminolevulinic acid (ALA) on the production of extracellular ALA was examined for the cells of soil derived Rhodospirillum rubrum N-1 belonged to the genus Rhodospirillaceae. The extracellular yield of ALA was increased to 23 fold (45 mg/l) from the basal condition (Lascelles' medium without L-glutamate) by successive addition of LA at initial (10 mM) and mid-log stage (30 mM) of cell cultivation. In addition to initial/mid-log mutual supplementations of LA (10 mM/30 mM) and glutamate (30/30 mM), respectively, by means of alternative feeding 10 mM $C_4$-precursors at mid-log phase of culture the extracellular ALA content was reached to 75 mg/l (40 fold).

• Journal of the Korea Organic Resources Recycling Association
• /
• v.5 no.1
• /
• pp.63-69
• /
• 1997

The role of L-glutamic acid, a precursor of $C_5$ ALA biosynthetic pathway, on the production of 5-aminolevulinic acid (ALA) has been described in cells of Rhodospirillum rubrum N-1. To the Lascelles basal medium the addition of both 30 mM L-glutamicacid and 20 mM levulinic acid (LA) provided to increase the extracellular ALA yield up to 40 fold (76 mg/l). By the addition of both 60 mM glycine and succinic acid, precursorsof $C_4$ ALA biosynthetic pathway, at middle log phase of cell growth ALA yield was increased 27 fold (52 mg/l) although the celt growth was inhibited to a certain extent.

• Proceedings of the Microbiological Society of Korea Conference
• /
• 2002.10a
• /
• pp.221.1-221.1
• /
• 2002

• Microbiology and Biotechnology Letters
• /
• v.16 no.6
• /
• pp.510-516
• /
• 1988

The effects of input substrate concentration and dilution rate on mass transfer resistance in the operation of immobilized cell reactors were investigated using Rhodospirillum rubrum KS-301 immobilized by Ca alginate as reactor element and glucose as growth-limiting substrate. The kinetic parameters were obtained to estimate effectiveness factors. In the packed-bed reactor, internal mass transfer resistance was predominating although external resistance could not be neglected. The overall effectiveness factor was decreased with increase of dilution rate. In the continuous stirred-tank reactor, external resistance was nearly neglected and the overall effectiveness factor was not affected by dilution rate. In this experiment the overall effectiveness factors in PBR and CSTR were estimated to be 0.70 and 0.71 at D$_{i}$ = 0.2/h, R = 0.15 cm, and S$_{i}$ : 1.0g/L, respectively.

• Journal of Microbiology and Biotechnology
• /
• v.17 no.9
• /
• pp.1460-1468
• /
• 2007

In this study, an approx. 2.5-kb gene fragment including the catalase gene from Rhodospirillum rubrum S1 was cloned and characterized. The determination of the complete nucleotide sequence revealed that the cloned DNA fragment was organized into three open reading frames, designated as ORF1, catalase, and ORF3 in that order. The catalase gene consisted of 1,455 nucleotides and 484 amino acids, including the initiation and stop codons, and was located 326 bp upstream in the opposite direction of ORF1. The catalase was overproduced in Escherichia coli UM255, a catalase-deficient mutant, and then purified for the biochemical characterization of the enzyme. The purified catalase had an estimated molecular mass of 189 kDa, consisting of four identical subunits of 61 kDa. The enzyme exhibited activity over a broad pH range from pH 5.0 to pH 11.0 and temperature range from $20^{\circ}C$ to $60^{\circ}C$C. The catalase activity was inhibited by 3-amino-1,2,4-triazole, cyanide, azide, and hydroxylamine. The enzyme's $K_m$ value and $V_{max}$ of the catalase for $H_2O_2$ were 21.8 mM and 39,960 U/mg, respectively. Spectrophotometric analysis revealed that the ratio of $A_{406}$ to $A_{280}$ for the catalase was 0.97, indicating the presence of a ferric component. The absorption spectrum of catalase-4 exhibited a Soret band at 406 nm, which is typical of a heme-containing catalase. Treatment of the enzyme with dithionite did not alter the spectral shape and revealed no peroxidase activity. The combined results of the gene sequence and biochemical characterization proved that the catalase cloned from strain S1 in this study was a typical monofunctional catalase, which differed from the other types of catalases found in strain S1.

• Microbiology and Biotechnology Letters
• /
• v.13 no.3
• /
• pp.303-309
• /
• 1985

Continuous production of hydrogen by Ca alginate-immobilized photosynthetic bacteria was studied in a packed-bed bioreactor. The dilution rate and input concentration of carbonaces substrate were selected as operating parameters. To choose the strain for immobilization, hydrogen productivities of Rhodopseudomonas caposulata 10006 and Rhodospirillum rubrum KS-301 were compared through preliminary batch cultures of their free cells: the former was found to show better hydrogen productivity in spite of its lower specific growth rate. For the continuous production of hydrogen by immobilized R capsulata, the optimum dilution rate was about 0.84 h$^{-1}$ . The Immobilized tells gave better hydrogen yield and conversion efficiency than free ones. And a kinetic parameter K'$_{m}$ was determined for the packed-bed bioreactor, being practically constant for a specific range of dilution rates.s.