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Han Dae Yun 3 Articles
Diversity of indigenous endophytic bacteria associated with the roots of Chinese cabbage (Brassica campestris L.) cultivars and their antagonism towards pathogens
Md. Azizul Haque , Han Dae Yun , Kye Man Cho
J. Microbiol. 2016;54(5):353-363.   Published online April 20, 2016
DOI: https://doi.org/10.1007/s12275-016-5641-7
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AbstractAbstract PDF
The study aimed to reveal the diversity of endophytic bacteria in the roots of Chinese cabbage (CC) cultivated in two areas in Korea, namely, Seosang-gun (SS) and Haenam-gun (HN), and also in a transgenic plant (TP) from the laboratory. A total of 653 colonies were isolated from the interior of CC roots, comprising 118, 302, and 233 isolates from SS, HN, and TP samples, respectively. Based on 16S rRNA gene sequence analysis, the isolates belonged to four major phylogenetic groups: high-G+C Gram-positive bacteria (HGC-GPB), low-G+C Gram-positive bacteria (LGC-GPB), Proteobacteria, and Bacteriodetes. The most dominant groups in the roots of the SS, HN, and TP cultivars were LGC-GPB (48.3%), Proteobacteria (50.2%), and HGC-GPB (38.2%), respectively. Importantly, most of the isolates that produced cell-walldegrading enzymes belonged to the genus Bacillus. Bacillus sp. (HNR03, TPR06), Bacillus pumilus (SSR07, HNR11, TPR07), and Bacillus subtilis (TPR03) showed high antagonism against the tested food-borne pathogenic bacteria. In addition, Bacillus sp. (HNR03, TPR06), Bacillus pumilus (SSR07, HNR11, HNR17, TPR11), Microbacterium oxidans (SSR09, TPR04), Bacillus cereus HNR10, Pseudomonas sp. HNR13, and Bacillus subtilis (TPR02, TPR03) showed strong antagonistic activity against the fungi Phythium ultimum, Phytophthora capsici, Fusarium oxysporum, and Rhizoctonia solani. The endophytes isolated from the TP cultivar showed the strongest antagonistic reactions against pathogens. This study is the first report on endophytic bacteria from Chinese cabbage roots.

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    Journal of Applied Biological Chemistry.2019; 62(4): 441.     CrossRef
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    Systematic and Applied Microbiology.2018; 41(6): 629.     CrossRef
  • Biocontrol of the internalization of Salmonella enterica and Enterohaemorrhagic Escherichia coli in mung bean sprouts with an endophytic Bacillus subtilis
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    International Journal of Food Microbiology.2017; 250: 37.     CrossRef
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    African Journal of Biotechnology.2016; 15(25): 1299.     CrossRef
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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    The ISME Journal.2025;[Epub]     CrossRef
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    International Journal of Systematic and Evolutionary Microbiology .2025;[Epub]     CrossRef
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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.

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