• Title/Summary/Keyword: C. sp

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Ceramium riosmenae sp. nov. (Ceramiaceae, Rhodophyta): a new complete corticated species on Gracilaria from Baja California Sur, Mexico

  • Won, Boo-Yeon;Cho, Tae-Oh
    • ALGAE
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    • v.26 no.4
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    • pp.289-297
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    • 2011
  • Ceramium riosmenae sp. nov. is described from Baja California Sur, Mexico based on morphological and molecular data. The new species is characterized by erect thalli only, penetrating rhizoids on Gracilaria, 7-8 periaxial cells, five cortical initials per periaxial cell, complete cortication throughout, an average of 11-12 segments between branching points, rare adventitious branchlets, and cruciate tetrasporangia. Although C. riosmenae sp. nov. is similar to C. interruptum, C. sinicola, and C. codicola reported from Baja California Sur, Mexico in size and habit, it differs from these species in the number of cortical initials, habit, degree of cortication, host, and the shape of rhizoidal tips. C. riosmenae is separated from C. interruptum with interrupted cortication and four cortical initials from C. sinicola with spins near the apex and incomplete cortication near the base and from C. codicola with bulbous rhizoids on Codium. Our rbcL sequences reveal sufficient sequence divergence (2.4-3.9%) between C. riosmenae and C. interruptum, C. sinicola, and C. codicola to warrant species recognition and to separate C. riosmenae from these species on a phylogenetic tree.

Identification and Cultural Characterization of Lipase Production Bacteria Isolated from Pond Effluent Sedimentary Layer (양식장 배출수 퇴적층에서 분리된 리파아제 생산 박테리아의 동정 및 배양학적 특성)

  • Kim, Man-Chul;Jang, Tae-Won;Harikrishnan, Ramasamy;Jang, Ik-Soo;Yeo, In-Kyu;Jeong, Joon-Bum;Heo, Moon-Soo
    • Korean Journal of Microbiology
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    • v.45 no.1
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    • pp.58-62
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    • 2009
  • From the course of screening of useful enzyme producing microorganism from marine sedimentary layer, we isolated 2 lipase producing strains and their lipase producing activities were tested. 16S rDNA sequence analysis showed that they were Gram-positive bacteria grouped on Janibacter sp. An excellent lipase producing strain, Janibacter sp. LI-68 and J. sp. LI-80 identified by 16S rDNA analysis and biochemical methods (BIOLOG), was further studied its lipase producing characteristics. The optimum initial pH, temperature and the optimum cultral time for the enzyme production on MA medium were 8, $30{\sim}40^{\circ}C$ and 96 h, respectively.

Purification and Characterization of Lipase from Acinetobacter sp. B2 Isolated from Oil­contaminated Soil (유류오염지역에서 분리한 Acinetobacter sp. B2로부터의 Lipase 정제 및 특성)

  • Son Seung Hwa;Park Kyeong Ryang
    • Korean Journal of Microbiology
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    • v.40 no.4
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    • pp.320-327
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    • 2004
  • Three hundreds thirty two bacterial colonies which were able to degrade crude oil were isolated from soil sam­ples that were contaminated with oil in Daejeon area. Among them, one bacterial strain was selected for this study based on its higher oil degrading ability, and this selected bacterial strain was identified as Acinetobactor sp. B2 through physiological-biochemical tests and analysis of its 16S rRNA sequence. Acinetobactor sp. B2 was able to utilize various carbohydrates but did not utilize trehalose and mannitol as a sole carbon source. Acinetobactor sp. B2 showed a weak resistance to antibiotics such as kanamycin, streptomycin, tetracycline and spectinomycin, but showed a high resistance up to mg/ml unit to heavy metals such as Ba, Li, Mn, AI, Cr and Pb. The optimal growth temperature of Acinetobactor sp. B2 was $30^{\circ}C.$ The lipase produced by Acinetobactor sp. B2 was purified by ammonium sulfate precipitation, DEAE-Toyopearl 650M ion exchange chromatography and Sephadex gel filtration chromatography. Its molecular mass was about 60 kDa and condition for the optimal activity was observed at $40^{\circ}C$ and pH 10, respectively. The activation energy of lipase for the hydrolysis of p­nitrophenyl palmitate was 2.7 kcal/mol in the temperature range of 4 to $37^{\circ}C,$ and the enzyme was unstable at the temperature higher than $60^{\circ}C.$ The Michaelis constant $(K_m)\;and\;V_{max}$ for p-nitrophenyl palmitate were 21.8 uM and $270.3\;{\mu}M\;min^{-1}mg^{-1},$ respectively. This enzyme was strongly inhibited by 10 mM $Cd^{2+},\;Co^{2+},\;Fe^{2+},\;Hg^{2+},$ EDTA and 2-Mercaptoethalol.

Expanded IL-22+ Group 3 Innate Lymphoid Cells and Role of Oxidized LDL-C in the Pathogenesis of Axial Spondyloarthritis with Dyslipidaemia

  • Hong Ki Min;Jeonghyeon Moon;Seon-Yeong Lee;A Ram Lee;Chae Rim Lee;Jennifer Lee;Seung-Ki Kwok;Mi-La Cho;Sung-Hwan Park
    • IMMUNE NETWORK
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    • v.21 no.6
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    • pp.43.1-43.14
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    • 2021
  • Group 3 innate lymphoid cells (ILC3), which express IL-22 and IL-17A, has been introduced as one of pathologic cells in axial spondyloarthritis (axSpA). Dyslipidaemia should be managed in axSpA patients to reduce cardiovascular disease, and dyslipidaemia promotes inflammation. This study aimed to reveal the role of circulating ILC3 in axSpA and the impact of dyslipidaemia on axSpA pathogenesis. AxSpA patients with or without dyslipidaemia and healthy control were recruited. Peripheral blood samples were collected, and flow cytometry analysis of circulating ILC3 and CD4+ T cells was performed. The correlation between Ankylosing Spondylitis Disease Activity Score (ASDAS)-C-reactive protein (CRP) and circulating immune cells was evaluated. The effect of oxidized low-density lipoprotein cholesterol (oxLDL-C) on immune cell differentiation was confirmed. AxSpA human monocytes were cultured with with oxLDL-C, IL-22, or oxLDL-C plus IL-22 to evaluate osteoclastogenesis using tartrate-resistant acid phosphatase (TRAP) staining and real-time quantitative PCR of osteoclast-related gene expression. Total of 34 axSpA patients (13 with dyslipidaemia and 21 without) were included in the analysis. Circulating IL-22+ ILC3 and Th17 were significantly elevated in axSpA patients with dyslipidaemia (p=0.001 and p=0.034, respectively), and circulating IL-22+ ILC3 significantly correlated with ASDAS-CRP (Rho=0.4198 and p=0.0367). Stimulation with oxLDL-C significantly increased IL-22+ ILC3, NKp44- ILC3, and Th17 cells, and these were reversed by CD36 blocking agent. IL-22 and oxLDL-C increased TRAP+ cells and osteoclast-related gene expression. This study suggested potential role of circulating IL-22+ ILC3 as biomarker in axSpA. Furthermore, dyslipidaemia augmented IL-22+ ILC3 differentiation, and oxLDL-C and IL-22 markedly increased osteoclastogenesis of axSpA.

Isolation and Characterization of Serratia sp. JM Producing Chitinase (Chitinase를 생성하는 Serratia sp. JM의 분리 및 특성)

  • 차진명;진상기고한철이인화
    • KSBB Journal
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    • v.11 no.1
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    • pp.92-98
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    • 1996
  • A chitinase-producing bacterium was isolated from seashore mud around Beobseongpo in Chunnam province by selective enrichment culture, and among it, one isolate which was the best in producing of chitinase was selected. Nutrient or MacConkey medium was confirmed with secreting of prodigiosin pigment by Serratia sp. JM, and it was performed by the production of clear zone on medium containing chitin. Serratia sp. JM was almost same compared with Serratia marcescens ATCC 27117 in respect of its morphological, physiological and biochemical characteristics except succinic, urea and pyruvic acid. Serratia sp. JM was resistant to tetracycline but was not resistant to kanamycin and chloramphenicol. The optimal temperature and pH for the production of chitinase from Serratia sp. JM were $30^{\circ}C$ and 7.5, respectively. Production of chitinase and pH in the medium increased until the cultivation of 120 hours, but after 120 hours, they were decreased due to the acetic acid accumulated from degradation of chitin by Serratia sp. JM.

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Characterization and Modeling of Growth Properties of Petroleum Desulfurizing Bacterium Desulfovibrio sp. B5 (석유탈황 미생물 Desulfovibrio sp. B5의 생육특성과 성장 Modeling)

  • 신철수;김명동;안장우;신평균;서진호
    • KSBB Journal
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    • v.14 no.1
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    • pp.45-50
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    • 1999
  • This study was focused on investigating the growth properties of a sulfate reducing bacterium Deslfovibrio sp. B5 which has metabolic ability for desulfurization of petroleum. The optimal temperature and pH for growth of Desulfovibiro sp. B5 were $38^{\circ}C$ and 6.6-7.0, respectively. Addition of 10% corn steep liquor to the Postgate medium C resulted in 0.79 g/L cell concentration, corresponding to a 1.8-fold increase in dry cell mass. Acetate concentrations above 10g/$\ell$ inhibited cell growth significantly. $H_2S$ generated from the sulfate reduction also inhibited the growth of Desulfovibrio sp. B5 at a concentration of 10mM total sulfide. But $N_2$ gassing relieved the growth inhibition by $H_2$S and thereby resulted in a 1.75-fold enhancement in specific growth and lactate consumption pattern of Desulfovibrio sp. B5.

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AUA as a Translation Initiation Site In Vitro for the Human Transcription Factor Sp3

  • Hernandez, Eric Moore;Johnson, Anna;Notario, Vicente;Chen, Andrew;Richert, John R.
    • BMB Reports
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    • v.35 no.3
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    • pp.273-282
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    • 2002
  • Sp3 is a bifunctional transcription factor that has been reported to stimulate or repress the transcription of numerous genes. Although the size of Sp3 mRNA is 4.0kb, the size of the known Sp3 cDNA sequence is 3.6kb. Thus, Sp3 functional studies have been performed with an artificially introduced start codon, and thus an amino-terminus that differs from the wild-type. Ideally, full-length cDNA expression vectors with the appropriate start codon should be utilized for these studies. Using 5'rapid amplification of cDNA ends, a full-length Sp3 cDNA clone was generated and the sequence verified in nine cell lines. No AUG initiation codon was present. However, stop codons were present in all three frames 5' to the known coding sequence. In vitro translation of this full-length cDNA clone produced the expected three isoforms-one at 100 kDa and two in the mid 60 kDa range. Electrophoretic mobility shift assays showed that the protein products had the ability to bind to the Sp1/3 consensus sequence. In vitro studies, using our Sp3 clone and site directed mutagenesis, identified the translation initiation site for the larger isoform as AUA. AUA has not been previously described as an endogenous initiation codon in eukaryotes.

Isolation of Alkalopsychrotrophic Protease-Producing Pseudomonas sp. RP-222 and Properties of Its Crude Enzyme (저온.알칼리성 Protease를 생산하는 Pseudomonas sp. RP-222의 분리 및 조효소의 특성)

  • 노종수;정영철;성낙계;박석규
    • Microbiology and Biotechnology Letters
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    • v.19 no.4
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    • pp.383-389
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    • 1991
  • In order to produce alkaline protease, psychrotrophic bacterium which have high enzyme activity at low temperature, was isolated by using enrichment culture from various samples and identified as genus alkalopsychrotropic Pseudomonas sp. RP-222. The optimal culture conditions for enzyme production were pH- 10.0, temperature-$20^{\circ}C$ and culture time-4 days. The optimum pH and temperature for the enzyme activity were pH 10.5 and $40^{\circ}C$, respectively and the enzyme was relatively stable at pH 7.0~13.0 and below $50^{\circ}C$. The enzyme was inhibited by ethylenediaminetetraacetate and phenylmethylsulfonylfluoride, indicating that the enzyme was a serine metalloenzyme, but considerably stable in the presence of surface active agents. Activity of the enzyme was increased by the addition of 0.05% Na-$\alpha$-olefin sulfonate.

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Utilization the Tofu-Residue for Production of the Bacteriocin 1. Cultural Conditions of Bacillus sp. for Amylase (박테리오신의 생산을 위한 두부비지의 이용 1. 두부비지에서 분리한 Bacillus sp.에 의한 Amylase의 생산조건)

  • 이선희;이명숙
    • Journal of Food Hygiene and Safety
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    • v.15 no.3
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    • pp.271-276
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    • 2000
  • A amylase producing bacteria were isolated from tofu residue and identified as Bacillus sp. according to the morphological and biochemical properties, which were named Bacillus sp. GM7330 and Bacillus sp. GM7312. The cultural condition for the production of amylase was showed on 5% tofu residue added 3% glucose and 0.15% yeast extract. And incubated during 72 hrs at 30。C, Bacillus sp. GM7330 and Bacillus sp. GM7312 were producing amylase of 488 units and 341 units.

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The Physiological and Biochemical Studies of Nocardia sp (Part I) Cell Fine Structure of Nocardia sp (Nocardia sp의 생이생화학적연구 (제1보) Nocardia sp의 미세구조에 관하여)

  • 홍순덕
    • Microbiology and Biotechnology Letters
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    • v.5 no.3
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    • pp.133-140
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    • 1977
  • The results of electron microscopic studies on the cell fine structure of Nocardia sp the location of tellurite-reducing enzyme and the reduction part of T. T. C. (Triphenyl tetrazonium chloride) were summarized as follows. As the fine structure of the cell, the membrane-like structure with unit membrane was distributed in the cytoplasm. The membrane-like structure had complicate forms: some of membrane-like structure appeared spiral form. As the metal tellurium salt appeared in the cytoplasm, it is obvious that tellurite and tellurate-reducing enzymes are present in the cytoplasm. Reduction of T. T. C. took place in the cell membrane and the intracellular membrane-like structure. Therefore, it was thought that reduction of tellurate and T. T. C. took place in different parts. T. T. C. formazane formed in the cell was reoxidized by osmic acid which was used as a fixation reagent for the electron microscopic specimen preparation. As 95% T. T. C. formazane was soluble in ethanol and embedding materials and removed out of the cell, an originally formed formazane appeared as electron light part on the electron microscopic image.

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