• 제목/요약/키워드: Aeromonas sp.

검색결과 48건 처리시간 0.019초

토양에서 분리한 Aeromonas sp 로 부터 \beta-mannanase 유전자의 클로닝 (Cloning of \beta-mananase gene from Aeromonas sp. in E. coli)

  • 박봉환;강대경;김하근
    • 한국미생물·생명공학회지
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    • 제29권4호
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    • pp.201-205
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    • 2001
  • 자연계로부터 locust bean gum이 들어 있는 선택배지에서 투명환을 형성하는 mannan 분해능을 갖는 미생물을 스크링 하였고 이를 Aeromonas sp. 로 동정하였다. Aero monas sp. 로부터 염색체 DNA를 분리하여 EcoRI으로 절단하여 대장균에 형질전환한 후 대장균 콜로니 주위에서 locust bean gum을 분해하여 투명환을 형성하는 대장균을 찾아냈다. 형질전환된 대장균으로부터 플라스미드를 분리하여 동일한 제한효소를 처리하여 확인한 결과 10 kd의 Aeromonas sp. 염섹체 DNA에 $\beta$-mannanase 유전자 존재하였다. 대장균에서 발현된 $\beta$-mannanase 의최적 반응 pH와 최적 반응온도는 각각 6.0과 $50^{\circ}C$로서 모균인 Aeromonas sp. 와 동일하였다.

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Aeromonas sp. MN44의 특성과 망간 산화에 관한 연구 (A Study on the Manganese Oxidation and Characteristics of Aeromonas sp)

  • 구종서;박경량
    • 생명과학회지
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    • 제15권1호
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    • pp.94-99
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    • 2005
  • 충청남도 목천과 충청북도 오창 근교의 토양으로부터 망간을 산화하는 64 집락을 분리하고 이 중 망간 산화능이 가장 우수한 한 균주를 최종 선별하여 생리, 생화학적 특성을 조사하고, 16S rRNA 염기 서열분석 등을 통하여 동정한 결과 최종 선별된 균주는 Aeromonas sp. MN44로 확인되었다. 최종 선별된 Aeromenas sp. MN44는 lactose를 제외한 여러 당들은 이용하지 못하였으며, 중금속내성은 lithium과 manganese에 대해서는 mg/ml 단위의 높은 농도까지 중금속 내성을 가지고 있었지만 cadmium에는 전혀 내성을 나타내지 않았다. 또 kanamycin, chloramphenicol, ampicillin, tetracycline, spectinomycin등 조사한 모든 항생제에 대해 전혀 내성을 갖지 않았다. Aeromonas sp. MN44가 생성하는 망간산화물질의 최적 pH는 pH 7.4로 확인되었으며, 이 균이 생성하는 망간 산화 factor는 proteinase K와 가열처리에 의해 저해되는 단백질이고, ammonium sulfate 침전과 ion exchange chromatography 그리고 gel filtration의 단계를 통해 부분 정제한 망간 산화 factor의 분자량은 약 113 kDa로 확인되었다.

어병(魚病) 세균(細菌)에 대한 쑥 정유(精油)의 항균력(抗菌力) 검색 (Antimicrobial activity of Artemisia princeps var. orientalis essential oil against fish pathogenic bacteria)

  • 김영길;노범진;이근광
    • 한국어병학회지
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    • 제7권2호
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    • pp.113-117
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    • 1994
  • 어병 세균에 대해 쑥(Artemisia princeps var. orientalis) 추출물인 정유의 항균성을 조사하였다. Aeromonas hydrophila, Aeromonas salmonicida, Aeromonas sorbia, Edwardsiella tarda 와 Streptococcus sp. (yellowtail)는 1,000~2,000 ppm 에서 증식이 억제되었다. 즉 억제 농도는 A.salmonicida 가 1,000 ppm A.hydrophila, A. sorbia, E. tarda 와 Streptococcus sp. (yellowtail)는 1,500 ppm 이었다. 그러나 Vibrio anguillarum, Vibrio ordalii, Edwardsiella ictaluri와 Streptococcus sp. (SF-1)는 100~2,000 ppm 농도에서 현저한 억제 효과는 없었다.

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녹차 카테킨 EGCG의 노출에 따른 식중독 세균인 용혈성 Aeromonas sp. MH-8의 특성조사 (Characterization of Hemolytic Aeromonas sp. MH-8 Responding to the Exposure of Green Tea Catechin, EGCG)

  • 김동민;오계헌
    • KSBB Journal
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    • 제31권4호
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    • pp.228-236
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    • 2016
  • The aim of this study was to characterize the hemolytic Aeromonas sp. MH-8 exposed to green tea catechin, epigallocatechin gallate (EGCG). Initially, the hemolytic Aeromonas sp. MH-8 was enriched and isolated from stale fish. Bactericidal effects of MH-8 exposed to EGCG ranging from 1 mg/mL to 4 mg/mL were monitored, and complete bactericidal effects were achieved within 3 h at 3 mg/mL and higher concentrations. SDS-PAGE with silver staining revealed that the amount of lipopolysaccharides increased or decreased in the strain MH-8 treated to different concentrations and exposing periods of EGCG in exponentially growing cultures. The stress shock proteins (70-kDa DnaK and 60-kDa GroEL), which might contribute to enhancing the cellular resistance to the cytotoxic effect of EGCG, were induced at different concentrations of EGCG exposed to cell culture of MH-8. Scanning electron microscopic analysis demonstrated the presence of irregular rod shapes with umbilicated surfaces for cells treated with EGCG. 2-DE of soluble protein fractions from MH-8 cultures showed 18 protein spots changed by EGCG exposure. These proteins involved in chaperons (e.g., DnaK, GroEL and trigger factor), enterotoxins (e.g., aerolysin and phospholipase C precursor), LPS synthesis (e.g., LPS biosynthesis protein and outer membrane protein A precursor), and various biosynthesis and energy metabolism were identified by peptide mass fingerprinting using MALDI-TOF. In consequence, EGCG was found to have substantial antibacterial effects against food-poisoning causing bacterium, hemolytic Aeromonas sp. MH-8. Also the results provide clues for understanding the mechanism of EGCG-induced stress and cytotoxicity on Aeromonas sp. MH-8.

Cellulase Activity of Symbiotic Bacteria from Snails, Achatina fulica

  • Kim, Jon Young;Yoon, Sae Min;Kim, Yeong-Suk
    • Journal of the Korean Wood Science and Technology
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    • 제43권5호
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    • pp.628-640
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    • 2015
  • Cellulase is the key enzyme in the use of cellulose-based biomaterials. Because of its structure, cellulose is difficult to be degraded by enzymes. In order to utilize cellulose-based biomaterials efficiently, evolutionary wisdom of how to use enzymes accurately and harmoniously in a biological system is needed, such as the cellulose digestive system in animals. In this study, the symbiotic bacteria from snails, Achatina fulica, were identified and their cellulase activity was evaluated. The 16S rRNA sequence analysis of 100 aerobic bacteria showed that they belonged to 9 genus and almost half of the bacteria were Lactococcus spp. Among 100 identified strains, only two Aeromonas sp. strains showed cellulase activity. Aeromonas sp. KMBS020 had both endo-${\beta}$-glucanase and ${\beta}$-glucosidase activities but Aeromonas sp. KMBS018 had ${\beta}$-glucosidase activity only. None of the 100 bacterial colonies had any cellobiohydrolase activity.

Isolation and Characterization of a Chitinolytic Enzyme Producing Marine Bacterium, Aeromonas sp. J-5003

  • Choi Yong Un;Kang Ji Hee;Lee Myung Suk;Lee Won Jae
    • Fisheries and Aquatic Sciences
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    • 제6권1호
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    • pp.1-6
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    • 2003
  • A chitinolytic enzyme-producing bacterium was isolated from sea water on the coast of Busan. The bacterium was identified as Aeromonas sp. based on its morphological, cultural and biochemical characteristics and designated Aeromonas sp. J-5003. The strain produced two chitinoloytic enzymes: chitinase and chitobiase. The optimum culture conditions of the strain for production of chitinoloytic enzymes were investigated. For the production of chitinase, the major components of medium were colloidal chitin $0.5\%$, glucose $0.2\%$, yeast extract $0.25\%$ and peptone $0.25\%$ while for the production of chitobiase, they were colloidal chitin $0.5\%$, galactose and tryptone $0.2\%$. The optimum cultural temperature and initial pH for the production of chitinase and chitobiase were $30^{\circ}C$ and pH 7.0, respectively.

난분해성 할로겐 치환 Phenol의 분해 (Biodegradation of Recalcitrant Halogen Substituted-Phenol)

  • 이건;이상준;이종근
    • 한국환경보건학회지
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    • 제18권2호
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    • pp.92-101
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    • 1992
  • Halogen substituted-phenol and analog phenol degrading strains were identified as Aeromonas, Moraxella, and Flavobacterium genus. Optimal degrading condition was generally 50~100 $\mu$M substituted-phenol as carbon source, $NH_4NO_3$ as nitrogen source, 30$\circ$C , and initial pH 7.2. $\rho$-Chlorophenol degrading strain of Aeromonas sp. C4 had biodegradability to the various substituted-phenols. Flavobacterium sp. M9 had substrate specificity to methyl substituted-function. Catechol was cleavaged by catechol 1, 2-dioxygenase in Aeromonas sp. C4, Moraxella sp. N7, and Flavobacterium sp. M9.

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CO2를 고정하는 화학독립영양미생물인 Aeromonas sp. strain JS-1의 Form I Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase 정제 및 특성 파악 (Form I Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase from CO2-Fixing Chemoautotrophic bacterium, Aeromonas sp. strain JS-1: Purification and Properties)

  • 나숙현;배상옥;정수정;정선용
    • KSBB Journal
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    • 제25권6호
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    • pp.559-564
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    • 2010
  • A new hydrogen-oxidizing bacterium, Aeromonas sp. strain JS-1, that can fix $CO_2$ via the reductive pentose phosphate cycle (Calvin-Benson cycle) under chemoautotrophic conditions but not photoautotrophic conditions was isolated from fresh water. Strain JS-1 showed considerable $CO_2$ fixation ability during continuous cultivation even at high $CO_2$ concentration. Strain JS-1 used $H_2$ and $CO_2$ fixation as energy and carbon sources, respectively. Carbon dioxide fixation is carried out through the Calvin-Benson cycle, in which ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) is the key enzyme. Hydrogen-oxidizing chemoautotrophic Aeromonas sp. strain JS-1 exhibited remarkedly strong RubisCO [EC 4.1.1.39] activity. RubisCO was purified as an $L_8S_8$-type hexadecamer with molecular mass of 560 kDa by gel filtration. The enzyme consisted of two different subunits eight large (56 kDa) and eight small (15 kDa), as demonstrated by SDS-PAGE. The specific activity of the purified enzyme was about 3.31 unit/mg and stable up to $45^{\circ}C$. The $K_m$ values for RuBP, $CO_2$, and $Mg^{2+}$ were estimated to be 0.25 mM, 5.2 mM and 0.91 mM, respectively.

내수 양식어와 인체에서 분리한 Aerornonas hydrophila의 병원성에 관한 연구 (The Pathogenicity of Aeromonas hydrophila Isolated from Freshwater fish and Human)

  • 이명원;김호훈;이연태;맹은호
    • 환경위생공학
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    • 제6권1호
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    • pp.31-46
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    • 1991
  • Aeromonas hydrophila which bacause various diseases in human also infects fresh water fish, severly damaging the fishing industries. To prevent disease in humans and reduce damaging on the fishing industries, We have examined several characteristics of Aeromonas hydrophila and obtained the following results. All of the strains gave a posive voges-proskauer, methyl-red, salicin and esculin reaction. Seventeen(94.4%) A. hydrophila strains presented the phenotype SP-PAB- in autoagglut-ination test, but only strain AH 997 showed $SP^{+}PAB^{+}$. in autoagglut ination test, but only strain AH 997 $SP^{+}PAB^{+}$ All of the strains took up the censored to various degrees. Three of 18 strains showed positive reaction in crystal violet binding test. Hemolytic activity ranged from titers of 0 to 1/256. Seven of the 17(38.8%) A. hydrophila strains were positive in sucking mouse assay. Cytotoxin activity on vero and RK cells was displayed various titers.(1/2-1/1024)

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Purification and Characterization of Cold Active Lipase from Psychrotrophic Aeromonas sp. LPB 4

  • Lee, Han-Ki;Ahn, Min-Jung;Kwak, Sung-Ho;Song, Won-Ho;Jeong, Byeong-Chul
    • Journal of Microbiology
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    • 제41권1호
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    • pp.22-27
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    • 2003
  • A lipase from Aeromonas sp. LPB 4, a psychrotophile isolated from a sea sediment was purified and characterized. The lipase was purified 53.5 fold to a homogeneous state by acetone precipitation and QAE sephadex column chromatography and its molecular weight was determined to be 50 kDa by SDS-PAGE. The enzyme exhibited maximum activity at 10$^{\circ}C$ and was stable at temperatures lower than 50$^{\circ}C$. This lipase favored substrates containing medium carbon chain of acyl group, while too low and high carbon chain decreased its activity. The lipolytic activity of purified lipase was slightly increased by the addition of 0.1% detergent, but decreased by 1% of detergent. Butanol severely decreased the lipase activity while methanol increased the activity about 15%.