Journal of Microbiology

Ki-Hong Yoon

3 Articles

Paenibacillus telluris sp. nov., a Novel Phosphate-Solubilizing Bacterium Isolated from Soil: Jae-Chan Lee , Chang-Jin Kim , Ki-Hong Yoon; J. Microbiol. 2011;49(4):617-621. Published online September 2, 2011; DOI: https://doi.org/10.1007/s12275-011-0471-0

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A phosphate-solubilizing bacterial strain designated PS38T was isolated from farm soil. The isolate was a Gram-positive, motile, endospore-forming, rod-shaped bacterium. It grew optimally at 37oC and pH 7.5. The predominant cellular fatty acids were anteiso-C15:0, anteiso-C17:0, and iso-C16:0. The DNA G+C content was 49.5 mol% and the predominant menaquinone was MK-7. Phylogenetic analyses based on 16S rRNA gene sequences showed that the strain PS38T belonged to the genus Paenibacillus and was most closely related to Paenibacillus chibensis JCM 9905T, P. barengoltzii SAFN-016T, P. timonensis 2301032T, and P. motobuensis MC10T with 96.3%, 96.0%, 95.9%, and 95.5% 16S rRNA gene sequence similarity, respectively. On the basis of morphological, chemotaxonomic, physiological, and phylogenetic properties, strain PS38T represents a novel species of the genus Paenibacillus, for which the name Paenibacillus telluris sp. nov. is proposed. The type strain is PS38T (=KCTC 13946T =CGMCC 1.10695T).

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Characterization of the Bacillus subtilis WL-3 Mannanase from a Recombinant Escherichia coli: Ki-Hong Yoon , Seesub Chung , Byung-Lak Lim; J. Microbiol. 2008;46(3):344-349. Published online July 5, 2008; DOI: https://doi.org/10.1007/s12275-008-0045-y

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Abstract PDF

A mannanase was purified from a cell-free extract of the recombinant Escherichia coli carrying a Bacillus subtilis WL-3 mannanase gene. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. Optimal conditions for the purified enzyme occurred at pH 6.0 and 60°C. The specific activity of the purified mannanase was 5,900 U/mg on locust bean gum (LBG) galactomannan at pH 6.0 and 50°C. The activity of the enzyme was slightly inhibited by Mg2+, Ca2+, EDTA and SDS, and noticeably enhanced by Fe2+. When the enzyme was incubated at 4°C for one day in the presence of 3 mM Fe2+, no residual activity of the mannanase was observed. The enzyme showed higher activity on LBG and konjac glucomannan than on guar gum galactomannan. Furthermore, it could hydrolyze xylans such as arabinoxylan, birchwood xylan and oat spelt xylan, while it did not exhibit any activities towards carboxymethylcellulose and para-nitrophenyl-β-mannopyranoside. The predominant products resulting from the mannanase hydrolysis were mannose, mannobiose and mannotriose for LBG or mannooligosaccharides including mannotriose, mannotetraose, mannopentaose and mannohexaose. The enzyme could hydrolyze mannooligosaccharides larger than mannobiose.

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Isolation of Novel Pseudomonas diminuta KAC-1 Strain Producing Glutaryl 7-Aminocephalosporanic Acid Acylase: Dae-Weon Kim , Sang-Mo Kang , Ki-Hong Yoon; J. Microbiol. 1999;37(4):200-205.

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Abstract PDF: 7-Aminocephalosporanic acide (7-ACA) is the initial compound in preparation of cephalosporin antibiotics widely used in clinical treatment. Bacteria producing glyutaryl 7-ACA acylase, which convert cephalosporin C to 7-ACA, has been screened in soil samples. A bacterial strain exhibiting high glutaryl 7-ACA acylase activity, designated KAC-1, was isolated and identified as a strain of Pseudomonas diminuta by characterizing its morphological and physiological properties. The screening procedures include culturing on enrichment media containing glutaric acid, glutamate, and glutaryl 7-aminocephalosporanic acid as selective carbon sources. To enhance enzyme production, optimal cultivation conditions were investigated. This strain grew optimally at pH 7 to 9 and in temperatures of 20 to 40 C, but acylase production was higher when the strain was grown at 25 C. Glutaric acid, glutamate and glucos also acted as inducers for acylase production. In a jar fermenter culture, P. diminuta KAC-1 produce acylase in a growth-associated manner. The substrate specificity of KAC-1 acylase by cell extract showed that this enzyme had specificity toward glutaryl 7-ACA, glutaryl 7-ADCA, but not cephalosporin C.

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