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- Niabella ginsenosidivorans sp. nov., isolated from compost
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Kwon-Jung Yi , Wan-Taek Im , Dong-Woon Kim , Qing Mei Liu , Soo-Ki Kim
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J. Microbiol. 2015;53(11):762-766. Published online October 28, 2015
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DOI: https://doi.org/10.1007/s12275-015-5463-z
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Abstract
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A Gram-reaction negative, strictly aerobic, non-motile, orange
colored, and rod-shaped bacterium (designated BS26T) isolated
from compost, was characterized by a polyphasic approach
to clarify its taxonomic position. Strain BS26T was
observed to grow optimally at 25–30°C and at pH 7.0 on
R2A and nutrient media. Strain BS26T showed β-glucosidase
activity that was responsible for its ability to transform ginsenoside
Rb1 (one of the active components of ginseng) to
ginsenoside compound-K (C-K). Phylogenetic analysis based
on 16S rRNA gene sequences indicated that strain BS26T belongs
to the genus Niabella of family Chitinophagaceae and
was most closely related to Niabella soli DSM 19437T (94.5%
similarity), N. yanshanensis CCBAU 05354T (94.3%), and
N. aurantiaca DSM 17617T (93.8%). The G+C content of genomic
DNA was 47.3 mol%. Chemotaxonomic data [predominant
isoprenoid quinone-MK-7, major fatty acids–iso-C15:0,
iso-C15:1 G, iso-C17:0 3-OH, and summed feature 3 (comprising
C16:1 ω7c and/or C16:1 ω6c)] supported the affiliation of
strain BS26T to the genus Niabella. However, strain BS26T
could be differentiated genotypically and phenotypically
from the recognized species of the genus Niabella. The novel
isolate therefore represents a novel species, for which the
name Niabella ginsenosidivorans sp. nov. is proposed, with
the type strain BS26T (=KACC 16620T =JCM 18199T).
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Citations
Citations to this article as recorded by

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Ling Zhang, Chuansheng Geng, Xingjuan Chen, Letian Chen, Tongchu Deng, Meiying Xu
Current Microbiology.2024;[Epub] CrossRef - Niabella beijingensis sp. nov. and Thermomonas beijingensis sp. nov., two bacteria from constructed wetland
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International Journal of Systematic and Evolutionary Microbiology
.2022;[Epub] CrossRef - List of new names and new combinations previously effectively, but not validly, published
Aharon Oren, George M. Garrity
International Journal of Systematic and Evolutionary Microbiology
.2019; 69(5): 1247. CrossRef - Niabella hibiscisoli sp. nov., isolated from soil of a Rose of Sharon garden
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International Journal of Systematic and Evolutionary Microbiology.2016; 66(8): 2774. CrossRef
- Cloning and Functional Characterization of Endo-β-1,4-Glucanase Gene from Metagenomic Library of Vermicompost
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Muhammad Yasir , Haji Khan , Syed Sikander Azam , Amar Telke , Seon Won Kim , Young Ryun Chung
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J. Microbiol. 2013;51(3):329-335. Published online June 28, 2013
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DOI: https://doi.org/10.1007/s12275-013-2697-5
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Scopus
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Abstract
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In the vermicomposting of paper mill sludge, the activity of earthworms is very dependent on dietetic polysaccharides including cellulose as energy sources. Most of these polymers are degraded by the host microbiota and considered potentially important source for cellulolytic enzymes. In the present study, a metagenomic library was constructed from vermicompost (VC) prepared with paper mill sludge and dairy sludge (fresh sludge, FS) and functionally screened for cellulolytic activities. Eighteen cellulase expressing clones were isolated from about 89,000 fosmid clones libraries. A short fragment library was constructed from the most active positive clone (cMGL504) and one open reading frame (ORF) of 1,092 bp encoding an endo-β-1,4-glucanase was indentified which showed 88% similarity with Cellvibrio mixtus cellulase A gene. The endo-β-1,4-glucanase cmgl504 gene was overexpressed in Escherichia coli. The purified recombinant cmgl504 cellulase displayed activities at a broad range of temperature (25–55°C) and pH (5.5–8.5). The enzyme degraded carboxymethyl cellulose (CMC) with 15.4 U, while having low activity against avicel. No detectable activity was found for xylan and laminarin. The enzyme activity was stimulated by potassium chloride. The deduced protein and three-dimensional structure of metagenomederived cellulase cmgl504 possessed all features, including general architecture, signature motifs, and N-terminal signal peptide, followed by the catalytic domain of cellulase belonging to glycosyl hydrolase family 5 (GHF5). The cellulases cloned in this work may play important roles in the degradation of celluloses in vermicomposting process and could be exploited for industrial application in future.
- Mucilaginibacter composti sp. nov., with Ginsenoside Converting Activity, Isolated from Compost
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Chang-Hao Cui , Tae-Eun Choi , Hongshan Yu , Fengxie Jin , Sung-Taik Lee , Sun-Chang Kim , Wan-Taek Im
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J. Microbiol. 2011;49(3):393-398. Published online June 30, 2011
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DOI: https://doi.org/10.1007/s12275-011-1176-0
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37
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37
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Abstract
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The Gram-negative, strictly aerobic, non-motile, non-spore-forming, rod shaped bacterial strain designated TR6-03T was isolated from compost, and its taxonomic position was investigated by using a polyphasic approach. Strain TR6-03T grew at 4-42°C and at pH 6.0-8.0 on R2A and nutrient agar without NaCl supplement. Strain TR6-03T had β-glucosidase activity, which was responsible for its ability to transform ginsenoside Re (one of the dominant active components of ginseng) to Rg2. On the basis of 16S rRNA gene sequence similarity, strain TR6-03T was shown to belong to the family Sphingobacteriaceae and to be related to Mucilaginibacter lappiensis ANJLI2T (96.3% sequence similarity), M. dorajii FR-f4T (96.1%), and M. rigui WPCB133T (94.1%). The G+C content of the genomic DNA was 45.6%. The predominant respiratory quinone was MK-7 and the major fatty acids were summed feature 3 (comprising C16:1 ω7c and/or iso-C15:0 2OH), iso-C15:0 and iso-C17:0 3OH. DNA and chemotaxonomic data supported the affiliation of strain TR6-03T to the genus Mucilaginibacter. Strain TR6-03T could be differentiated genotypically and phenotypically from the recognized species of the genus Mucilaginibacter. The isolate therefore represents a novel species, for which the name Mucilaginibacter composti sp. nov. is proposed, with the type strain TR6-03T (=KACC 14956T =KCTC 12642T =LMG 23497T).