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Hoon Kim 3 Articles
Chitinibacter suncheonensis sp. nov., a Chitinolytic Bacterium from a Mud Flat in Suncheon Bay
Sung Kyum Kim , Yong Ho Kim , Yu Seok Jeong , Han Beur Na , Jungho Kim , Keun Sik Baik , Han Dae Yun , Jung-Kul Lee , Hoon Kim
J. Microbiol. 2012;50(6):1058-1062.   Published online December 30, 2012
DOI: https://doi.org/10.1007/s12275-012-2333-9
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AbstractAbstract PDF
A chitinolytic bacterium, designated strain SK16T, was isolated from a mud flat in Suncheon Bay, Republic of Korea. Strain SK16T is Gram-negative, strictly aerobic, motile by a polar flagellum, and short rod-shaped. Phylogenetic analyses based on 16S rRNA gene sequences showed that the strain belonged to the genus Chitinibacter and was most closely related to Chitinibacter tainanensis S1T (98.2% similarity). DNA-DNA hybridization analyses showed a low association value of 20.45±4.08% between them. The major cellular fatty acids, the G+C content of the genomic DNA, and the predominant quinone of the strain were summed feature 3 (iso-C15:0 2-OH and/or C16:1 ω7c; 50.5%) and C12:0 (12.5%), 52.26 mol%, and Q-8, respectively. Based on the phylogenetic, chemotaxonomic, and phenotypic properties, strain SK16T represents a novel species of the genus Chitinibacter, for which the name Chitinibacter suncheonensis sp. nov. is proposed. The type strain is SK16T (=KCTC 23839T =DSM 25421T).

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Citations to this article as recorded by  
  • Characterization of a novel Bi-functional cold-adapted chitinase from Chitinibacter mangrovi FCG-7T for efficient production of N-acetyl-D-glucosamine
    Chenxi Gu, Liyan Yang, Susu Han, Dengfeng Yang, Xiaodong Xu, WenChao Zhang, Mingguo Jiang, Lixia Pan
    Food Bioscience.2026; 75: 108168.     CrossRef
  • Impact of moisture on microbial decomposition phenotypes and enzyme dynamics
    Nicholas J Reichart, Sheryl Bell, Vanessa A Garayburu-Caruso, Natalie Sadler, Sharon Zhao, Kirsten S Hofmockel
    The ISME Journal.2025;[Epub]     CrossRef
  • Validation List no. 226: valid publication of new names and new combinations effectively published outside the IJSEM
    Aharon Oren, Markus Göker
    International Journal of Systematic and Evolutionary Microbiology .2025;[Epub]     CrossRef
  • Molecular Characterization of Four Alkaline Chitinases from Three Chitinolytic Bacteria Isolated from a Mudflat
    Sung Kyum Kim, Jong Eun Park, Jong Min Oh, Hoon Kim
    International Journal of Molecular Sciences.2021; 22(23): 12822.     CrossRef
  • The Draft Genome Sequence and Analysis of an Efficiently Chitinolytic Bacterium Chitinibacter sp. Strain GC72
    Alei Zhang, Xiaofang Mo, Guoguang Wei, Ning Zhou, Sai Yang, Jie Chen, Yingying Wang, Kequan Chen, Pingkai Ouyang
    Current Microbiology.2020; 77(12): 3903.     CrossRef
  • Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation
    Cong Gao, Alei Zhang, Kequan Chen, Zhikui Hao, Junmao Tong, Pingkai Ouyang
    Biochemical Engineering Journal.2015; 97: 59.     CrossRef
The Role of Carbohydrate-Binding Module (CBM) Repeat of a Multimodular Xylanase (XynX) from Clostridium thermocellum in Cellulose and Xylan Binding
Thangaswamy Selvaraj , Sung Kyum Kim , Yong Ho Kim , Yu Seok Jeong , Yu-Jeong Kim , Nguyen Dinh Phuong , Kyung Hwa Jung , Jungho Kim , Han Dae Yun , Hoon Kim
J. Microbiol. 2010;48(6):856-861.   Published online January 9, 2011
DOI: https://doi.org/10.1007/s12275-010-0285-5
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AbstractAbstract PDF
A non-cellulosomal xylanase from Clostridium thermocellum, XynX, consists of a family-22 carbohydratebinding module (CBM22), a family-10 glycoside hydrolase (GH10) catalytic module, two family-9 carbohydrate-binding modules (CBM9-I and CBM9-II), and an S-layer homology (SLH) module. E. coli BL21(DE3) (pKM29), a transformant carrying xynX', produced several truncated forms of the enzyme. Among them, three major active species were purified by SDS-PAGE, activity staining, gel-slicing, and diffusion from the gel. The truncated xylanases were different from each other only in their C-terminal regions. In addition to the CBM22 and GH10 catalytic modules, XynX1 had the CBM9-I and most of the CBM9-II, XynX2 had the CBM9-I and about 40% of the CBM9-II, and XynX3 had about 75% of the CBM9-I. The truncated xylanases showed higher binding capacities toward Avicel than those toward insoluble xylan. XynX1 showed a higher affinity toward Avicel (70.5%) than XynX2 (46.0%) and XynX3 (42.1%); however, there were no significant differences in the affinities toward insoluble xylan. It is suggested that the CBM9 repeat, especially CBM9-II, of XynX plays a role in xylan degradation in nature by strengthening cellulose binding rather than by enhancing xylan binding.

Citations

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  • Xylanases from Cellulomonas sp. B6 Produce Xylooligosaccharides with Prebiotic Potential from Agro-Industrial Byproducts
    Ornella Mailén Ontañon, Hebe Mónica Dionisi, Juliana Topalian, Laura Emilce Navas, Caio Cesar de Mello Capetti, María Esperanza Cerón Cucchi, Victoria Mariel Hracek, Laura Faas, Adam Dowle, Igor Polikarpov, Marina Ciancia, Leonardo Dario Gómez, Eleonora C
    Journal of Agricultural and Food Chemistry.2026;[Epub]     CrossRef
  • Eggshell-zeolite composite additive enhances humification and mitigates CH4 emissions during cow-manure composting: Insights from metagenomic analysis
    Hongbo Zhang, Jinbiao Gao, Haolong Wu, Yufeng Chen, Xiang He, Xueqin He
    Environmental Technology & Innovation.2026; 43: 105058.     CrossRef
  • Structure-Informed Insights into Catalytic Mechanism and Multidomain Collaboration in α-Agarase CmAga
    Yuxian You, Bee Koon Gan, Min Luo, Xinzhe Zheng, Nanqing Dong, Yixiong Tian, Caiming Li, Haocun Kong, Zhengbiao Gu, Daiwen Yang, Zhaofeng Li
    Journal of Agricultural and Food Chemistry.2025; 73(13): 7975.     CrossRef
  • Cellulolytic and hemicellulolytic capacity of Acetivibrio clariflavus
    Katarína Šuchová, Vladimír Puchart
    Applied Microbiology and Biotechnology.2025;[Epub]     CrossRef
  • Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10
    Nicole Torosian, Jonathan K. Covington, Allison M. Cook, Nancy O. Nou, Marike Palmer, Ritesh Mewalal, Miranda Harmon‐Smith, Ian K. Blaby, Jan‐Fang Cheng, Matthias Hess, Brian P. Hedlund
    FEBS Open Bio.2025; 15(10): 1629.     CrossRef
  • Cellulosomal hemicellulases: Indispensable players for ensuring effective lignocellulose bioconversion
    Min Xiao, Ya-Jun Liu, Edward A. Bayer, Akihiko Kosugi, Qiu Cui, Yingang Feng
    Green Carbon.2024; 2(1): 57.     CrossRef
  • Whole-genome sequencing and genomic analysis of four Akkermansia strains newly isolated from human feces
    Wenjing Lu, Biqing Zha, Jie Lyu, Chenxi LingHu, Jing Chen, Sisi Deng, Xiangling Zhang, Liang Li, Guoqing Wang
    Frontiers in Microbiology.2024;[Epub]     CrossRef
  • Carbohydrate binding modules: Compact yet potent accessories in the specific substrate binding and performance evolution of carbohydrate-active enzymes
    Yuxian You, Haocun Kong, Caiming Li, Zhengbiao Gu, Xiaofeng Ban, Zhaofeng Li
    Biotechnology Advances.2024; 73: 108365.     CrossRef
  • Xylan-breakdown apparatus of Clostridium thermocellum
    Pedro R. V. Hamann, Eliane F. Noronha
    Cellulose.2022; 29(14): 7535.     CrossRef
  • Exploration of the key functional proteins from an efficient cellulolytic microbial consortium using dilution-to-extinction approach
    Qinghua Zhang, Hanguang Li, Xiangdong Zhu, Fenju Lai, Zhijun Zhai, Yuanxiu Wang
    Journal of Environmental Sciences.2016; 43: 199.     CrossRef
  • Biochemical characterization of a novel thermostable GH11 xylanase with CBM6 domain from Caldicellulosiruptor kronotskyensis
    Weibo Qiao, Shuge Tang, Shuofu Mi, Xiaojing Jia, Xiaowei Peng, Yejun Han
    Journal of Molecular Catalysis B: Enzymatic.2014; 107: 8.     CrossRef
  • Thermophilic lignocellulose deconstruction
    Sara E. Blumer-Schuette, Steven D. Brown, Kyle B. Sander, Edward A. Bayer, Irina Kataeva, Jeffrey V. Zurawski, Jonathan M. Conway, Michael W. W. Adams, Robert M. Kelly
    FEMS Microbiology Reviews.2014; 38(3): 393.     CrossRef
  • An evolutionary analysis of the GH57 amylopullulanases based on the DOMON_glucodextranase_like domains
    Yu‐Liang Jiao, Shu‐Jun Wang, Ming‐Sheng Lv, Yao‐Wei Fang, Shu Liu
    Journal of Basic Microbiology.2013; 53(3): 231.     CrossRef
  • Purification, Characterization of GH11 Endo-β-1,4-xylanase from Thermotolerant Streptomyces sp. SWU10 and Overexpression in Pichia pastoris KM71H
    Warin Deesukon, Yuichi Nishimura, Tatsuji Sakamoto, Wasana Sukhumsirichart
    Molecular Biotechnology.2013; 54(1): 37.     CrossRef
  • Recombinant production and characterization of full-length and truncated β-1,3-glucanase PglA from Paenibacillussp. S09
    Rui Cheng, Jinping Chen, Xiaohong Yu, Yang Wang, Shiming Wang, Jianfa Zhang
    BMC Biotechnology.2013;[Epub]     CrossRef
  • Production of XynX, a Large Multimodular Protein of Clostridium thermocellum, by Protease-Deficient Bacillus subtilis Strains
    Nguyen Dinh Phuong, Yu Seok Jeong, Thangaswamy Selvaraj, Sung Kyum Kim, Yong Ho Kim, Kyung Hwa Jung, Jungho Kim, Han Dae Yun, Sui-Lam Wong, Jung-Kul Lee, Hoon Kim
    Applied Biochemistry and Biotechnology.2012; 168(2): 375.     CrossRef
  • Biochemical and Structural Insights into Xylan Utilization by the Thermophilic Bacterium Caldanaerobius polysaccharolyticus
    Yejun Han, Vinayak Agarwal, Dylan Dodd, Jason Kim, Brian Bae, Roderick I. Mackie, Satish K. Nair, Isaac K.O. Cann
    Journal of Biological Chemistry.2012; 287(42): 34946.     CrossRef
  • A thermostable GH45 endoglucanase from yeast: impact of its atypical multimodularity on activity
    Marie Couturier, Julia Feliu, Mireille Haon, David Navarro, Laurence Lesage-Meessen, Pedro M Coutinho, Jean-Guy Berrin
    Microbial Cell Factories.2011;[Epub]     CrossRef
Use of Sucrose-Agar Globule with Root Exudates for Mass Production of Vesicular Arbuscular Mycorrhizal Fungi
Thangaswamy Selvaraj , Hoon Kim
J. Microbiol. 2004;42(1):60-63.
DOI: https://doi.org/1998 [pii]
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AbstractAbstract PDF
A sucrose-agar globule (SAG) was newly introduced to increase production of the vesicular arbuscular mycorrhizal (VAM) fungal spores, Gigaspora gigantea and Glomus fasciculatum. An SAG inoculum and a sucrose-agar globule with root exudates (SAGE) inoculum were prepared, and their spore productions were compared with a soil inoculum. When the SAGE was used as the inoculum on sucroseagar medium plates the number of spores was increased (35% more than the soil inoculum). After the soil inoculum and SAGE were inoculated on an experimental plant, Zingiber officinale, the percentage root colonization, number of VAM spores, and dry matter content were analyzed. It was observed that the SAGE showed a higher percentage of root colonization (about 10% more), and increases in the number of spores (about 26%) and dry matter (more than 13%) for the two VAM fungal spores than the soil inoculum. The results of this study suggested that the SAGE inoculum may be useful for the mass production of VAM fungi and also for the large scale production of VAM fungal fertilizer.

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