Ho-Yong Park

Korea Research Institute of Bioscience and Biotechnology KRIBB, Anzan, Gyeonggi Province, South Korea

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Publications (46)74.55 Total impact

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    ABSTRACT: The XylH gene (1167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that ofof an endo-β-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-β-1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multi-functional enzyme possessing endo-beta-1,4-xylanase activity together with beta-1,3/beta-1,4-glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylose-based polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.
    Journal of microbiology and biotechnology. 05/2014;
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    ABSTRACT: Arazyme is a novel extracellular metalloprotease secreted by Aranicola proteolyticus. Endothelial cells are involved in the pathogenesis of a number of inflammatory diseases, induce uncontrolled cell viability and express various inflammatory mediators, including cytokines, chemokines, adhesion molecules and reactive oxygen species (ROS). In the current study, human umbilical vein endothelilal cells (HUVECs) were used to investigate the anti‑inflammatory effects of arazyme following lipopolysaccharide (LPS) stimulation. Apoptosis of HUVECs due to LPS was inhibited by arazyme. In various inflammatory responses induced by LPS, arazyme inhibited the secretion of the monocyte chemoattractant protein‑1 and interleukin‑6, and the expression of vascular cell adhesion molecule‑1 and intercellular adhesion molecule‑1. Arazyme also suppressed ROS production in HUVECs. The action of arazyme was not associated with NF‑κB activity in HUVECs. These results indicate that arazyme has anti‑inflammatory properties in inflamed endothelial cells and may be useful as a therapeutic agent for inflammatory diseases associated with endothelial cells.
    Molecular Medicine Reports 05/2014; · 1.17 Impact Factor
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    ABSTRACT: In the present study, the inhibitory effect of arazyme on allergic inflammation was investigated by evaluating the alteration of cytokine production and expression of skin barrier proteins in immune and HaCaT human keratinocyte cells. THP‑1 human monocytic and EoL‑1 human eosinophilic cells were treated with Dermatophagoides pteronissinus extract (DpE). Monocyte chemotactic protein‑1 (MCP‑1)/CCL2, interleukin (IL)‑6 and IL‑8 increased following DpE treatment and arazyme significantly blocked the increase of MCP‑1, IL‑6 and IL‑8 expression in cell types. Secretion of MCP‑1, IL‑6 and IL‑8 induced by lipopolysaccharide in THP‑1 cells was also inhibited by arazyme treatment. Arazyme inhibited the secretion of IL‑6 and IL‑8 due to phorbol 12‑myristate 13‑acetate and calcium ionophores in human mast cells. Arazyme blocked the secretion of thymus and activation‑regulated chemokine (TARC)/CCL17, MCP‑1, IL‑6 and IL‑8 due to tumor necrosis factor‑α (TNF‑α) and interferon‑γ (IFN‑γ) in HaCaT cells. TNF‑α and IFN‑γ suppressed the expression of skin barrier proteins, including filaggrin, involucrin and loricrin. By contrast, arazyme increased the expression of filaggrin, involucrin and loricrin. These results may contribute to the development of a therapeutic drug for the treatment of allergic diseases, including atopic dermatitis.
    Molecular Medicine Reports 06/2013; · 1.17 Impact Factor
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    ABSTRACT: The XylP gene, which encodes endoxylanase in Bacillus sp. HY-20, was subcloned, and two expression plasmids, pG-xylP and pGMF-xylP were constructed. These plasmids, which contain different signal sequences, XylP s.s and s.s, respectively, for the secretory expression of endoxylanase, were transformed into Saccharomyces cerevisiae SEY2102 and FY833, respectively. The recombinant endoxylanases were successfully expressed, with a total activity range of 23.7-70.1 unit/ml according to the expression system and host strain. The endoxylanase activity in SEY2102/pGMF-xylP reached a maximum of 88.1 unit/ml in baffled flask culture. Most of the recombinant endoxylanase was efficiently secreted in the extracellular fraction, and the s.s was more efficient for secreting endoxylanase in yeast than the XylP s.s. Therefore, the expression system developed in this study produces large extracellular amounts of endoxylanase using S. cerevisiae as the host strain, and it could be used in bioethanol production and industrial applications.
    Journal of Life Science. 01/2013; 23(7).
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    ABSTRACT: The potential of non-ionic polysorbate surfactants as alternative inducers of medium-chain-length poly(3-hydroxyalkanoates) (MCL-PHAs) for the production of diverse bacterial MCL-PHA depolymerases was evaluated. When grown with corn oil as the sole carbon substrate, Pseudomonas alcaligenes LB19 preferentially produced lipolytic enzymes, but its MCL-PHA depolymerase was not induced by the substrate. However, the results of activity staining and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis clearly revealed that Tween 20 induced simultaneous production of lipolytic enzymes and the MCL-PHA depolymerase with the molecular mass (26.5 kDa) of P. alcaligenes LB19, which has been previously identified. Moreover, the co-production of two functionally distinct hydrolytic enzymes induced by Tween 20 was commonly observed in various Gram-positive and Gram-negative bacteria that were fed the substrate. Thus, it is expected that non-ionic polysorbate surfactants including Tween 20 can be widely exploited as promising universal substrates for the facile and efficient production of diverse MCL-PHA depolymerases.
    Bioresource Technology 07/2012; 121:47-53. · 4.75 Impact Factor
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    ABSTRACT: The gene (2304-bp) encoding a novel xylanolytic enzyme (XylK2) with a catalytic domain, which is 70% identical to that of Cellulomonas flavigena DSM 20109 GH6 β-1,4-cellobiohydrolase, was identified from an earthworm (Eisenia fetida)-symbiotic bacterium, Cellulosimicrobium sp. strain HY-13. The enzyme consisted of an N-terminal catalytic GH6-like domain, a fibronectin type 3 (Fn3) domain, and a C-terminal carbohydrate-binding module 2 (CBM 2). XylK2ΔFn3-CBM 2 displayed high transferase activity (788.3 IU mg(-1)) toward p-nitrophenyl (PNP) cellobioside, but did not degrade xylobiose, glucose-based materials, or other PNP-sugar derivatives. Birchwood xylan was degraded by XylK2ΔFn3-CBM 2 to xylobiose (59.2%) and xylotriose (40.8%). The transglycosylation activity of the enzyme, which enabled the formation of xylobiose (33.6%) and xylotriose (66.4%) from the hydrolysis of xylotriose, indicates that it is not an inverting enzyme but a retaining enzyme. The endo-β-1,4-xylanase activity of XylK2ΔFn3-CBM 2 increased significantly by approximately 2.0-fold in the presence of 50mM xylobiose.
    Bioresource Technology 03/2012; 107:25-32. · 4.75 Impact Factor
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    ABSTRACT: Strains RU-16(T), RU-28, RU-04(T) and PU-02(T) were isolated from the gut of the African mole cricket, Gryllotalpa africana. Phylogenetic analyses based on 16S rRNA gene sequences revealed that the strains belonged to the family Microbacteriaceae. All four strains were most closely related to Curtobacterium ginsengisoli DCY26(T) (below 97 % 16S rRNA gene sequence similarity). These isolates were Gram-stain-positive, motile (by gliding), rod-shaped and exhibited ivory-coloured colonies. Their chemotaxonomic properties included MK-11 as the major respiratory quinone, ornithine as the cell-wall diamino acid, acetyl as the acyl type of the peptidoglycan, cyclohexyl-C(17 : 0) as the major fatty acid and phosphatidylglycerol and diphosphatidylglycerol as the major polar lipids. On the basis of phenotypic, chemotaxonomic and phylogenetic analyses, we propose a new genus in the family Microbacteriaceae, Gryllotalpicola gen. nov., with three novel species, Gryllotalpicola daejeonensis sp. nov. (type strain RU-04(T)  = KCTC 13809(T)  = JCM 17590(T)), Gryllotalpicola koreensis sp. nov. (type strain RU-16(T)  = KCTC 13810(T)  = JCM 17591(T)) and Gryllotalpicola kribbensis sp. nov. (type strain PU-02(T)  = KCTC 13808(T)  = JCM 17593(T)). Gryllotalpicola koreensis is the type species of the genus. Additionally, we propose that Curtobacterium ginsengisoli should be reclassified in the genus as Gryllotalpicola ginsengisoli comb. nov. (type strain DCY26(T)  = KCTC 13163(T)  = JCM 14773(T)).
    INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY 11/2011; 62(Pt 10):2363-70. · 2.11 Impact Factor
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    ABSTRACT: The gene (1272-bp) encoding a β-1,4-mannanase from a gut bacterium of Eisenia fetida, Cellulosimicrobium sp. strain HY-13 was cloned and expressed in Escherichia coli. The recombinant β-1,4-mannanase (rManH) was approximately 44.0 kDa and has a catalytic GH5 domain that is 65% identical to that of the Micromonospora sp. β-1,4-mannosidase. The enzyme exhibited the highest catalytic activity toward mannans at 50 °C and pH 6.0. rManH displayed a high specific activity of 14,711 and 8498 IU mg⁻¹ towards ivory nut mannan and locust bean gum, respectively; however it could not degrade the structurally unrelated polysaccharides, mannobiose, or p-nitrophenyl sugar derivatives. rManH was strongly bound to ivory nut mannan, Avicel, chitosan, and chitin but did not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate). The superior biocatalytic properties of rManH suggest that the enzyme can be exploited as an effective additive in the animal feed industry.
    Bioresource Technology 06/2011; 102(19):9185-92. · 4.75 Impact Factor
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    ABSTRACT: A xylanolytic gut bacterium isolated from Eisenia fetida, Cellulosimicrobium sp. strain HY-13, produced an extracellular glycoside hydrolase capable of efficiently degrading mannose-based substrates such as locust bean gum, guar gum, mannotetraose, and mannopentaose. The purified mannan-degrading enzyme (ManK, 34,926 Da) from strain HY-13 was found to have an N-terminal amino acid sequence of DEATTDGLHVVDD, which has not yet been identified. Under the optimized reaction conditions of 50°C and pH 7.0, ManK exhibited extraordinary high specific activities of 7109 IU/mg and 5158 IU/mg toward locust bean gum and guar gum, respectively, while the enzyme showed no effect on sugars substituted with p-nitrophenol and various non-mannose carbohydrates. Thin layer chromatography revealed that the enzyme degraded locust bean gum to mannobiose and mannotetraose. No detectable amount of mannose was produced from hydrolytic reactions with the substrates. ManK strongly attached to Avicel, β-cyclodextrin, lignin, and poly(3-hydroxybutyrate) granules, but not bound to chitin, chitosan, curdlan, or insoluble oat spelt xylan. The aforementioned characteristics of ManK suggest that it is a unique endo-β-1,4-mannanase without additional carbohydrolase activities, which differentiates it from other well-known carbohydrolases.
    Enzyme and microbial technology. 04/2011; 48(4-5):365-70.
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    ABSTRACT: The virulence against the two-spotted spider mite, Tetranychus urticae Koch, was evaluated with entomopathogenic fungus Paecilomyces lilacinus (Thom) Samson HY-4 which is isolated from coleopteran insect and registered to Korean and US patents. Virulence tests were conducted with conidial suspensions () of P. lilacinus HY-4 against T. urticae adults and positive results were recorded in laboratory conditions. The spraying device was also developed for the efficient and exact evaluation of treatment. The developed spraying device was named as SD-tower sprayer and its efficacy of spraying conidia was evaluated. The accumulated mortality caused by P. lilacinus HY-4 using SD-tower spray was about 73% at 6 days after inoculation. This suggest that the isolate P. lilacinus HY-4 may be considered as promising for a new approach to prevent adult infestations by T. urticae.
    International Journal of Industrial Entomology. 01/2011; 22(1).
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    ABSTRACT: Pseudomonas fulva TY16 biosynthesized medium-chain-length poly(3-hydroxyalkanoates) (MCL-PHAs) containing unsaturated 3-hydroxydodecenoate unit (approximately 8-9%) when grown with volatile aromatic compounds including benzene, toluene, and ethylbenzene as sole carbon substrate. In particular, when cultivated using a continuous feeding system designed to supply toluene at a flow rate of 0.42gL(-1)h(-1) into a 7-L jar fermentor, the growth of the organism reached up to approximately 3.87gL(-1) after the 48h fed-batch fermentation, representing an accumulated cellular MCL-PHA of 58.9% by weight. The obtained MCL-PHA was a copolyester primarily consisting of 3-hydroxydecanoate (55.2%) and 3-hydroxyoctanoate (26.8%) with minor constituents being 3-hydroxyhexanoate (3.7%), 3-hydroxydodecenoate (8.2%), and 3-hydroxydodecanoate (6.1%). The present results suggest that P. fulva TY16 is a promising candidate for the biotechnological conversion of toxic petrochemical wastes to valuable biopolymers.
    Bioresource Technology 11/2010; 101(21):8485-8. · 4.75 Impact Factor
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    ABSTRACT: The novel intracellular GH10 xylanase (iXylC) gene (1023-bp) of Cohnella laeviribosi HY-21 encoded a protein consisting of 340 amino acids with a deduced molecular mass of 39,330Da and a calculated pI of 5.81. The primary structure of iXylC was 70% identical to that of Geobacillus sp. GH10 enzyme (GenBank accession number: EDV78425). Xylanolytic activity of the His-tagged iXylC overproduced in Escherichiacoli BL21 was stimulated by 2.2-fold in the presence of 0.5% non-ionic detergents. iXylC produced a mixture of xylooligosaccharides (xylobiose to xylooctaose) from xylotriose and xylotetraose used as the hydrolytic substrate. In addition, it exhibited considerable cleavage activities for p-nitrophenylxylopyranoside (PNP-xylopyranoside) and PNP-cellobioside, indicating that iXylC is a unique GH10 enzyme. The hydrolytic activity (57.8IUmL(-1)) of iXylC toward PNP-xylopyranoside increased to 8.3-fold by W217A and W315A mutations, while mutations of W133A, W295A, and W303A abolished the hydrolytic activity of the enzyme.
    Bioresource Technology 11/2010; 101(22):8814-21. · 4.75 Impact Factor
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    ABSTRACT: A novel GH10 endo-β-1,4-xylanase (XylG) gene from Streptomyces thermocarboxydus HY-15, which was isolated from the gut of Eisenia fetida, was cloned, over-expressed, and characterized. The XylG gene (1182 bp) encoded a polypeptide of 393 amino acids with a deduced molecular mass of 43,962 Da and a calculated pI of 6.74. The primary structure of XylG was 69% similar to that of Thermobifida fusca YX endo-β-1,4-xylanase. It was most active at pH 6.0 and 55 °C. The susceptibilities of xylans to XylG were as follows: oat spelt xylan > birchwood xylan > beechwood xylan. The XylG also showed high activity (474 IU/mg) toward p-nitrophenylcellobioside. Moreover, at pH 6.0 and 50 °C, the Vmax and Km values of the XylG were 127 IU/mg and 2.51 mg/ml, respectively, for oat spelt xylan and 782 IU/mg and 5.26 mM, respectively, for p-nitrophenylcellobioside. A homology model indicated that XylG folded to form a (β/α)8-barrel with two catalytic residues of an acid/base (Glu181) and a nucleophile (Glu289). The formation of a disulfide bond between Cys321 and Cys327 were predicted by homology modeling.
    Journal of Molecular Catalysis B: Enzymatic. 01/2010;
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    ABSTRACT: Burkholderia sp. IS-01 capable of biosynthesizing poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [poly(3HB-co-3HV)] copolyesters with a high molar fraction of 3HV was isolated from the gut of the adult longicorn beetle, Moechotypa diphysis. The strain IS-01 was relatively tolerant to high concentrations of levulinic acid and accumulated a poly(13.5 mol% 3HB-co-86.5 mol% 3HV) copolyester when cultivated on a mixture of gluconate (20 g/L) and levulinic acid (12.5 g/L). In this case, the content of the copolyester in the cells was approximately 60.0%. The compositions of the copolyesters were easily regulated by altering the molar ratio of gluconate and levulinic acid in the medium. The organism was found to possess a class I PHA synthase (PhaC) gene (1,881 bp) that encodes a protein with a deduced molecular mass of 68,538 Da that consists of 626 amino acids. The PhaC of this organism was most similar to that of B. cenocepacia PC184 (92% similarity).
    The Journal of Microbiology 10/2009; 47(5):651-6. · 1.28 Impact Factor
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    ABSTRACT: The gene encoding a novel modular xylanase from Cellulosimicrobium sp. strain HY-13 was identified and expressed in Escherichia coli, and its truncated gene product was characterized. The enzyme consisted of three distinct functional domains, an N-terminal catalytic GH10 domain, a fibronectin type 3 domain, and C-terminal carbohydrate-binding module 2.
    Applied and environmental microbiology 09/2009; 75(22):7275-9. · 3.69 Impact Factor
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    ABSTRACT: During a search for exo-enzyme-producing bacteria in the gut of an insect, Diestrammena apicalis, a novel bacterium capable of degrading pectin was isolated. The isolate, designated strain RCB-08(T), comprised Gram-positive, endospore-forming, motile rods capable of growth at 15-30 degrees C and pH 6.0-8.7. The DNA G+C content of the isolate was 51.5 mol% and the predominant cellular fatty acid was anteiso-C(15 : 0) (74.1 %). Phylogenetic analysis based on 16S rRNA gene sequences showed that strain RCB-08(T) was affiliated with a cluster within the Paenibacillaceae, and was related most closely to Paenibacillus chondroitinus NBRC 15376(T), with a sequence similarity of 96.7 %. The DNA-DNA relatedness value for strain RCB-08(T) with P. chondroitinus NBRC 15376(T) was 15.0 %. Strain RCB-08(T) hydrolysed pectin, but not cellulose, casein, starch or xylan. Strain RCB-08(T) could be clearly distinguished from other Paenibacillus species on the basis of characteristics observed using a polyphasic approach. Therefore strain RCB-08(T) is considered to represent a novel species of the genus Paenibacillus, for which the name Paenibacillus pectinilyticus sp. nov. is proposed. The type strain is RCB-08(T) (=KCTC 13222(T)=CECT 7358(T)).
    International journal of systematic and evolutionary microbiology 07/2009; 59(Pt 6):1342-7. · 2.11 Impact Factor
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    Bioorganic & Medicinal Chemistry Letters - BIOORG MEDICINAL CHEM LETTER. 01/2009; 19(6):1836-1836.
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    ABSTRACT: A xylanolytic bacterium, Cellulosimicrobium sp. HY-13, was isolated from the digestive tract of an earthworm, Eisenia fetida. The purified cellulase-free endo-β-1,4-xylanase (XylK) produced by strain HY-13 was found to contain an N-terminal amino acid sequence of APSTLEAAAE and to have a relative molecular mass of 36 kDa. It was most active at pH 6.0 and 55 °C and had Vmax and Km values toward oat spelt xylan of 4067 IU/mg and 2.78 mg/ml, respectively. XylK primarily degraded xylan to a series of xylooligosaccharides composed of xylobiose to xylotetraose, but it could not further hydrolyze xylobiose to xylose. The results of the present study suggest that the relatively highly active XylK lacking exo-xylanolytic activity is a promising candidate for the efficient production of non-digestible xylooligosaccharides that may have beneficial effects to gastrointestinal health via promotion of the growth of probiotics.
    Process Biochemistry 01/2009; 44(9):1055-1059. · 2.44 Impact Factor
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    ABSTRACT: An exo-symbiotic bacterium capable of hydrolyzing xylan was isolated from the gut of the mole cricket, Gryllotalpa orientalis, and identified as Cellulosimicrobium sp. HY-12. The xylanase (XylA( CspHY-12)) of this organism bound tightly to both DEAE and mono Q resins, and its molecular mass (M(r)) was about 39.0 kDa. The highest xylanase activity was observed at pH 6.0 and 60 degrees C. The enzyme was greatly suppressed by Ca(2+), Cu(2+), Co(2+), and Fe(2+) ions but not by Mg(2+) and Mn(2+). Although XylA( CspHY-12) was capable of hydrolyzing various types of xylosic compounds, it could not decompose carboxymethyl cellulose or xylobiose. The xylA (CspHY-12 ) gene consisted of an 1,188 bp open reading frame that encoded a polypeptide of 395 amino acids with a deduced molecular mass of 42,925 Da. The domain structure of XylA( CspHY-12) was most similar to those of the glycoside hydrolase (GH) family 10 endoxylanases. However its sequence identity with any of the enzymes in this family was below 52%. The results of this study suggest that the XylA( CspHY-12) is a new cellulase-free endo-beta-1,4-xylanase with some properties that are distinct from those of GH family 10.
    Antonie van Leeuwenhoek 06/2008; 93(4):437-42. · 2.07 Impact Factor
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    ABSTRACT: Arazyme is a novel protease produced by the HY-3 strain of Aranicola proteolyticus, which is a Gram-negative aerobic bacterium that has been isolated from the intestine of the spider Nephila clavata. This study focused on the hepatoprotective effect of Arazyme on carbon tetrachloride (CCl4)-induced acute hepatic injury in senescence marker protein 30 (SMP30) knock-out (KO) mice and SMP30 wild-type (WT) mice. WT mice and SMP30 KO mice were divided into eight groups as follows: (i) two negative control groups (G1, G5) which were treated with a single intraperitoneal (i.p.) olive oil injection. (ii) Two positive control groups (G2, G6) which received a single i.p. CCl4 (0.4mL/kg) injection. (iii) Two vitamin C-treated groups (G3, G7) which received a single oral administration of vitamin C (100mg/kg) and were injected with a single i.p. CCl4 (0.4mL/kg). (iv) Two Arazyme-treated groups (G4, G8) which received a single oral administration of Arazyme (500mg/kg) and were injected with a single i.p. CCl4 (0.4mL/kg). Through present study, we could find that Arazyme-treated groups showed decreased degree of liver injury, increased expression of SMP30, decreased expression of phospho-Smad3 (p-Smad3), elevated expression of antioxidant proteins including sorbitol dehydrogenase, dihydropteridine reductase (DHPR), dehydrofolate reductase (DHFR), NADH dehydrogenase, glutathione S-transferase kappa 1 (GSTK1) and phospholipid hydroperoxide glutathione peroxidase (PHGPx) compared with non-Arazyme-treated groups. Therefore, it is concluded that Arazyme plays a significant role in protecting injured hepatocytes by increasing the expression of SMP30, inhibiting the transforming growth factor-beta (TGF-beta)/Smad pathway and elevating the expression of antioxidant proteins.
    Toxicology 05/2008; 246(2-3):132-42. · 4.02 Impact Factor

Publication Stats

324 Citations
74.55 Total Impact Points

Institutions

  • 2001–2014
    • Korea Research Institute of Bioscience and Biotechnology KRIBB
      • • Industrial Bio-materials Research Center
      • • Insect Resources Laboratory
      Anzan, Gyeonggi Province, South Korea
  • 2010–2012
    • Chungnam National University
      • Department of Microbiology & Molecular Biology
      Seongnam, Gyeonggi, South Korea
  • 2005–2008
    • Kyungpook National University
      • • Department of Pathology
      • • College of Veterinary Medicine
      Daikyū, Daegu, South Korea