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Kwon, Young-Kyung,Kim, Ji Hyung,Kim, Jennifer Jooyoun,Yang, Sung-Hyun,Ye, Bo-Ram,Heo, Soo-Jin,Hyun, Jung-Ho,Qian, Zhong-Ji,Park, Heung-Sik,Kang, Do-Hyung,Oh, Chulhong Springer-Verlag 2014 Current microbiology Vol.69 No.4
<P>A strain designated as S85(T) was isolated from a seaweed collected from coastal area of Chuuk State in Micronesia. The strain was gram-negative, rod-shaped, and non-motile and formed yellow colonies on the SWY agar (0.2?% yeast extract and 1.5?% agar in seawater) and Marine agar 2216. The strain grew at pH 5-9 (optimum, pH 8), at 15-40?C (optimum, 25-28?C), and with 1-9?% (w/v) NaCl (optimum, 3?%). The phylogenetic analysis based on 16S rRNA gene sequence showed that strain S85(T) was related to Lutibacter litoralis CL-TF09(T) and Maritimimonas rapanae A31(T) with 91.4?% and with 90.5?% similarity, respectively. The dominant fatty acids were iso-C15:0, iso-C15:0 3-OH and iso-C17:0 3-OH, C16:0 3-OH and summed feature 3 (C16:1 ω7c and/or iso-C15:0 2-OH). The major isoprenoid quinone was MK-6. The DNA G+C content of the type strain was 34.6?mol?%. The major polar lipids were phosphatidylethanolamine, an unknown glycolipid and two unknown polar lipids. Based on this polyphasic taxonomic data, strain S85(T) stands for a novel species of a new genus, and we propose the name Ochrovirga pacifica gen. nov., sp. nov. The type strain of O. pacifica is S85(T) (=KCCM 90106 =JCM 18327(T)).</P>
Oh, Chulhong,Nikapitiya, Chamilani,Lee, Youngdeuk,Whang, Ilson,Kang, Do-Hyung,Heo, Soo-Jin,Choi, Young-Ung,Lee, Jehee Sociedade Brasileira de Microbiologia 2010 Brazilian journal of microbiology Vol.41 No.4
<P>An agar-degrading <I>Pseudoalteromonas</I> sp. AG52 bacterial strain was identified from the red seaweed <I>Gelidium amansii</I> collected from Jeju Island, Korea. A β-agarase gene which has 96.8% nucleotide identity to <I>Aeromonas</I> β-agarase was cloned from this strain, and was designated as a<I>ga</I>A. The coding region is 870 bp, encoding 290 amino acids and possesses characteristic features of the glycoside hydrolase family (GHF)-16. The predicted molecular mass of the mature protein was 32 kDa. The recombinant β-agarase (rAgaA) was overexpressed in <I>Escherichia coli</I> and purified as a fusion protein. The optimal temperature and pH for activity were 55 °C and 5.5, respectively. The enzyme had a specific activity of 105.1 and 79.5 unit/mg toward agar and agarose, respectively. The pattern of agar hydrolysis demonstrated that the enzyme is an endo-type β-agarase, producing neoagarohexaose and neoagarotetraose as the final main products.</P><P>Since, <I>Pseudoalteromonas</I> sp. AG52 encodes an a<I>ga</I>A gene, which has greater identity to <I>Aeromonas</I> β-agarase, the enzyme could be considered as novel, with its unique bio chemical characteristics. Altogether, the purified rAgaA has potential for use in industrial applications such as development of cosmetics and pharmaceuticals.</P>
Jeon, Mansik,Jenkins, Samir,Oh, Junghwan,Kim, Jeehyun,Peterson, Tara,Chen, Jingyi,Kim, Chulhong Future Medicine Ltd 2014 Nanomedicine Vol.9 No.9
<P>The objectives of this study were to demonstrate nonionizing photoacoustic tomography (PAT) of bladders with near-infrared absorbing gold nanocages (GNCs) as an optical-turbid tracer and to investigate the fate of GNCs after photoacoustic imaging.</P>