Journal of Microbiology

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The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT: Thinh-Phat Cao , Jin Myung Choi , Si Wouk Kim , Sung Haeng Lee; J. Microbiol. 2018;56(4):246-254. Published online February 28, 2018; DOI: https://doi.org/10.1007/s12275-018-7483-y

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The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MPT (MDHMas), was determined at 1.7 Å resolution. The active form of MDHMas (or MDHIMas) is a heterotetrameric α2β2, where each β-subunit assembles on one side of each of the α-subunits, in a symmetrical fashion, so that two β-subunits surround the two PQQ-binding pockets on the α-subunits. The active site consists of a PQQ molecule surrounded by a β-propeller fold for each α-subunit. Interestingly, the PQQ molecules are coordinated by a Mg2+ ion, instead of the Ca2+ ion that is commonly found in the terrestrial MDHI, indicating the efficiency of osmotic balance regulation in the high salt environment. The overall interaction of the β-subunits with the α-subunits appears tighter than that of terrestrial homologues, suggesting the efficient maintenance of MDHIMas integrity in the sea water environment to provide a firm basis for complex formation with MxaJMas or Cyt cL. With the help of the features mentioned above, our research may enable the elucidation of the full molecular mechanism of methanol oxidation by taking advantage of marine bacterium-originated proteins in the methanol oxidizing system (mox), including MxaJ, as the attainment of these proteins from terrestrial bacteria for structural studies has not been successful.

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Luteimonas dalianensis sp. nov., an Obligate Marine Bacterium Isolated from Seawater: Yanjuan Xin , Xupeng Cao , Peichun Wu , Song Xue; J. Microbiol. 2014;52(9):729-733. Published online August 2, 2014; DOI: https://doi.org/10.1007/s12275-014-3610-6

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Abstract

A marine bacterial strain, designated OB44-3T, was isolated from a crude oil-contaminated seawater sample collected near Dalian Bay, China. Cells of strain OB44-3T were Gramnegative, aerobic, rod-shaped, and oxidase- and catalasepositive. The major fatty acids were branched-chain saturated iso-C15:0 (27.9%) and unsaturated iso-C17:1 ω9c (14.8%). The DNA G+C content was 64.6 mol%. Phylogenetic analysis based on the 16S rRNA gene sequence indicated that strain OB44-3T was a member of the genus Luteimonas (95–96% 16S rRNA gene sequence similarity); its closest neighbors were the type strains of Luteimonas terricola (96% sequence similarity), Luteimonas mephitis (96%), and Luteimonas lutimaris (96%). On the basis of phenotypic, chemotaxonomic, and phylogenetic distinctiveness, strain OB44-3T was considered to represent a novel species of the genus Luteimonas. The name Luteimonas dalianensis sp. nov. is proposed, with strain OB44-3T (=CGMCC 1.12191T =JCM 18136T) as the type strain.

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International Journal of Systematic and Evolutionary Microbiology .2024;[Epub] CrossRef
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Luteimonas galliterrae sp. nov., isolated from poultry farm soil
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International Journal of Systematic and Evolutionary Microbiology .2023;[Epub] CrossRef
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Kristina Ulrich, Regina Becker, Undine Behrendt, Michael Kube, Volker Schneck, Andreas Ulrich
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Ya Chen, Ying Zhang, Di Xin, Xiaonan Luo, Huancheng Pang, Yuyi Li, Jianli Zhang
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Enhanced Production of Carboxymethylcellulase by a Marine Bacterium, Bacillus velezensis A-68, by Using Rice Hulls in Pilot-scale Bioreactor under Optimized Conditions for Dissolved Oxygen: Wa Gao , Hye-Jin Kim , Chung-Han Chung , Jin-Woo Lee; J. Microbiol. 2014;52(9):755-761. Published online July 30, 2014; DOI: https://doi.org/10.1007/s12275-014-4156-3

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Abstract

The optimal conditions for the production of carboxymethylcellulase (CMCase) by Bacillus velezensis A-68 at a flask scale have been previously reported. In this study, the parameters involved in dissolved oxygen in 7 and 100 L bioreactors were optimized for the pilot-scale production of CMCase. The optimal agitation speed and aeration rate for cell growth of B. velezensis A-68 were 323 rpm and 1.46 vvm in a 7 L bioreactor, whereas those for the production of CMCase were 380 rpm and 0.54 vvm, respectively. The analysis of variance (ANOVA) implied that the highly significant factor for cell growth was the aeration rate, whereas that for the production of CMCase was the agitation speed. The optimal inner pressures for cell growth and the production of CMCase by B. velezensis A-68 in a 100 L bioreactor were 0.00 and 0.04 MPa, respectively. The maximal production of CMCase in a 100 L bioreactor under optimized conditions using rice hulls was 108.1 U/ml, which was 1.8 times higher than that at a flask scale under previously optimized conditions.

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Esraa Abd Elhameed, Alaa R. M. Sayed, Tharwat E. E. Radwan, Gamal Hassan
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Enhanced Production of Carboxymethylcellulase by Recombinant Escherichia coli Strain from Rice Bran with Shifts in Optimal Conditions of Aeration Rate and Agitation Speed on a Pilot-Scale
Chung-Il Park, Jae-Hong Lee, Jianhong Li, Jin-Woo Lee
Applied Sciences.2019; 9(19): 4083. CrossRef
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Miao Ye, Xiangfang Tang, Ru Yang, Hongfu Zhang, Fangshu Li, Fangzheng Tao, Fei Li, Zaigui Wang
ACS Chemical Biology.2018; 13(3): 500. CrossRef
Comparison of optimal conditions for mass production of carboxymethylcellulase by Escherichia coli JM109/A-68 with other recombinants in pilot-scale bioreactor
Myung-Hwan Kim, Wa Gao, Chung-Han Chung, Jin-Woo Lee
Biotechnology and Bioprocess Engineering.2017; 22(2): 142. CrossRef
Construction of a recombinant Escherichia coli JM109/A-68 for production of carboxymethylcellulase and comparison of its production with its wild type, Bacillus velezensis A-68 in a pilot-scale bioreactor
Myung-Hwan Kim, Duk-Un Kang, Jin-Woo Lee
Biotechnology and Bioprocess Engineering.2016; 21(5): 601. CrossRef

Dasania marina gen. nov., sp. nov., of the Order Pseudomonadales, Isolated from Arctic Marine Sediment: Yoo Kyung Lee , Soon Gyu Hong , Hyun Hee Cho , Kyeung Hee Cho , Hong Kum Lee; J. Microbiol. 2007;45(6):505-509.; DOI: https://doi.org/2644 [pii]

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Abstract: An obligately aerobic bacterium, strain KOPRI 20902T, was isolated from a marine sediment in Ny-Ålesund, Spitsbergen Islands, Norway. Cells were irregular rods and motile with polar monotrichous flagellum. The optimum growth temperature was 17-22°C. Cells grew best in pH 7.0-10.0 and 3-4% sea salts (corresponding to 2.3-3.1% NaCl). The novel strain required Ca2+ or Mg2+ in addition to NaCl for growth. Sequence analysis of 16S rRNA gene revealed that the Arctic isolate is distantly related with established species (<92.4% sequence similarity) and formed a monophyletic group with Cellvibrio, which formed a distinct phylogenetic lineage in the order Pseudomonadales. Predominant cellular fatty acids [C16:1 ω7c/15:0 iso 2OH (45.3%), C16:0 (18.4%), ECL 11.799 (11.2%), C10:0 3OH (10.4%)]; DNA G+C content (37.0 mol%); nitrate reduction to nitrogen; absence of aesculin hydrolysis, N-acetyl-β-glucosaminidase and esterase; no assimilation of arabinose, galactose, glucose, lactose, maltose, and trehalose differentiated the strain from the genus Cellvibrio. Based on the phylogenetic and phenotypic characteristics, Dasania marina gen. nov., sp. nov. is proposed in the order Pseudomonadales. Strain KOPRI 20902T (=KCTC 12566T=JCM 13441T) is the type strain of Dasania marina.

The Influence of NaCl and Carbonylcyanide-m-Chlorophenylhydrazone on the Production of Extracellular Proteases in a Marine Vibrio Strain: Young Jae Kim; J. Microbiol. 2004;42(2):156-159.; DOI: https://doi.org/2028 [pii]

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Abstract: In general, the salinity of the ocean is close to 3.5% and marine vibrios possess the respiratory chainlinked Na+ pump. The influence of sodium chloride and the proton conductor carbonylcyanide m-chlorophenylhydrazone (CCCP) on the production of extracellular proteases in a marine Vibrio strain was examined. At the concentration of 0.5 M, sodium chloride minimally inhibited the activity of extracellular proteases by approximately 16%, whereas at the same concentration, the producton of extracellular proteases was severely inhibited. On the other hand, the production of extracellular proteases was completely inhibited by the addition of 2 μM CCCP at pH 8.5, where the respiratory chain-linked Na^+ pump functions.

Purification and Characterization of Chitinase from a Marine Bacterium, Vibrio sp. 98CJ11027: Shin Hye Park , Jung-Hyun Lee , Hong Kum Lee; J. Microbiol. 2000;38(4):224-229.

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Abstract: Chitin-degrading marine bacterial strain 98CJ11027 was isolated from bryozoa from the coastal area of Cheju Island, Korea, and identified as a member of the genus Vibrio. The molecular mass of the main extracellular chitinase (chitinase I), purified from strain 98CJ11027, was estimated to be 98 kDa. The optimal condition for chitinase I activity is pH 6.0 and 45 C. The activity was inhibited by Fe^+2 and Cu^+2. Chitinase I displayed the hydrolysis type of chitobiosidase and catalyzed reversed hydrolysis leading to the synthesis of tetraacetylchitotetraose.

Respiratory Chain-Linked Components of the Marine Bacterium Vibrio alginolyticus Affect Each Other: Young Jae Kim; J. Microbiol. 2002;40(2):125-128.

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Abstract: The aerobic respiratory chain of Vibrio alginolyticus possesses two different kinds of NADH oxidase systems, i.e., an Na^+ -dependent NADH oxidase system and an Na^+ -independent NADH oxidase system. When deamino-NADH, which is the only substrate for the Na^+ -dependent NADH oxidase system, was used as a substrate, the maximum activities of Na^+ -dependent NADH:quinone oxidoreductase and Na^+ -dependent NADH oxidase were obtained at about 0.06 M and 0.2 M NaCl, respectively. When NADH, which is a substrate for both Na^+ -dependent and Na^+ -independent NADH oxidase systems was used as a substrate, the NADH oxidase activity had a pH optimum at about 8.0. In contrast, when deamino-NADH was used as a substrate, the NADH oxidase activity had a pH optimum at about 9.0. On the other hand, inside-out membrane vesicles prepared from the wild-type bacterium generated only a very small [delta]pH by the NADH oxidase system, whereas inside-out membrane vesicles prepared from Nap1, which is a mutant defective in the Na^+ pump, generated [delta]pH to a considerable extent by the NADH oxidase system. On the basis of the results, it was concluded that the respiratory chain-linked components of V. alginolyticus affect each other.

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