• 유기물자원화
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• 제6권1호
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• pp.13-20
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• 1998

고농도 유기폐수인 양돈 폐수에 광합성 미생물(Rhodospirillum rubrum N-1)을 접종하고 여기에 공기를 160 mL/min 주입함으로써 양돈분뇨의 악취제거 효과를 조사하였다. 7일 동안 1일 간격으로 이화학적 변화를 검토하였다. 검토 결과 Biochemical Oxygen Demand (BOD) 20,000ppm인 양돈폐수의 경우 호기적 조건과, Rhodospirillum rubrum N-1 접종한 경우 volatile fatty acids(VFAs)의 제거율이 87.0%였으며, BOD제거율 54.6%, $PO_4-P$는 54.5%의 감소를 보였고, PH, $NH_3$ 등은 증가하는 경향을 나타내었다. T-N, T-P, $NO_3-N$, $NO_2-N$, $H_2S-N$, mercaptane 등은 별다른 증감율을 보이지 않고 일정하게 나타났다.

• Journal of Microbiology
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• 제39권3호
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• pp.168-176
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• 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
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• 제36권6호
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• pp.488-494
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• 1993

토양으로부터 생육도와 유기산의 자화도가 우수한 광합성세균 P17 균주를 분리하여 균학적 성질을 검토한 결과 이 균주는 Rhodospirillum rubrum으로 동정되었다. 유기폐수처리용 종균 생산을 위한 본 균주의 배양조건을 검토한 결과, 탄소원으로서 0.2% Na-acetate, 0.1% Na-propionate, 0.2% Na-lactate를 함유한 혼합 유기산이 효과적이었으며, 0.1% yeast extract를 첨가하였을 때 높은 생육도를 나타내었다. 최적배양조건의 환경인자들은 온도 $30^{\circ}C$, pH 7.0, 조도 2,500 lux, 교반 $50{\sim}100\;rpm$ 등이었다. Jar fermentor를 이용한 회분배양과 반연속배양으로부터 각각 5.17 g/l와 7.93 g/l의 균체가 생산되었으며, 연속배양에서는 희석비율 0.21 $h^{-1}$에서 생산성이 0.206 g/l/h이었다. R. rubrum P17을 두부공업폐수에 적용시켰을 때, 4일간 배양으로 초기 COD(3,240 mg/l)를 250 mg/l까지 감소시켰다.

• Journal of Microbiology
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• 제44권2호
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• pp.185-191
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• 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.

• 유기물자원화
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• 제5권1호
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• pp.25-32
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• 1997

토양에서 분리한 광합성 세균인 Rhodospirillum rubrum N-1 균주에 의한 ${\delta}$-aminolevulinic acid (ALA) 생산에 있어서 levulinic acid (LA) 및 ALA 생합성 경로의 첨가효과를 검토하였다. Glutamate를 제외한 Lascelles의 기본배지에 LA를 배양초기에 10mM, 이후 대수기 중기에 30 mM을 첨가한 결과 균체외의 ALA 생산성은 최고 45 mg/l 도달, LA 미첨가 대비 23배 증가하였다. ALA 생합성의 전구물질인 glycine-succinate ($C_4$) 및 glutamate ($C_5$)의 feeding 효과는 배양초기/대수기 중기에 LA 10/30 mM을, glutamate 30 mM/30 mM을 각각 첨가하는 한편, 대수기 중기에 10 mM 농도의 $C_4$ 전구물질을 별도로 첨가배양함으로써 미첨가 대비의 ALA 생산성이 약 40배 (75 mg/l) 증가하였다.

• 유기물자원화
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• 제5권1호
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• pp.63-69
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• 1997

5-Aminolevulinic acid (ALA) 생합성의 $C_5$ 경로의 전구물질인 L-glutamic acid가 Rhodospirillum rubrum N-1 새포내에서 ALA 생산의 역할을 검토하였다. Lascelles의 기본배지에 L-glutamic acid와 levulinic acid (LA)를 각각 30, 20 mM 첨가배양으로써 균체외 ALA 생산성이 40배 증가(76 mg/l)하였다. 한편 $C_4$ 경로의 기질인 glycine과 succinic acid를 대수기 중기에 각각 60 mM 첨가함으로써, 균의 증식은 억제되었으나 균체외의 ALA는 52 mg/l에 달하였다.

• 한국미생물학회:학술대회논문집
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• 한국미생물학회 2002년도 추계학술대회
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• pp.221.1-221.1
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• 2002

• 한국미생물·생명공학회지
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• 제16권6호
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• pp.510-516
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• 1988

본 연구는 균주로 Rhodospirillum rubrum KS-301, 증식 제한 기질로 글루코오스, 고정화 담체로 Ca alginate를 사용한 고정화 생물 반응기를 조작할 때 담체에 의해 형성되는 물질전달 저항에 대한 도입 기질의 농도, 희석속도의 영향을 고찰하였다. 또한 효율인자를 평가하기 위해 속도식 변수를 구하였다. 충전층 반응기의 경우 외부 액막 물질전달 저항보다는 내부 물질전달 저항이 우세함을 알 수 있었고 총괄 효율인자는 희석속도의 증가에 따라 감소하였다. 연속 교반 탱크 반응기의 경우 외부 액막 물질전달 저항은 무시할 수 있으며 총괄 효율인자는 희석속도에 영향을 받지 않았다. 희석속도 0.2/h, 비드 반경 0.15cm, 초기 글루코오스 농도 1.0g/L의 실험조건에서 총괄 효율인자는 충전층 반응기와 연속 교반 반응기에서 각각 0.70과 0.77이었다.

• Journal of Microbiology and Biotechnology
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• 제17권9호
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• pp.1460-1468
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• 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.

• 한국미생물·생명공학회지
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• 제13권3호
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• pp.303-309
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• 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.