Su Young Hong

Gyeongsang National University, Chinju, South Gyeongsang, South Korea

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Publications (27)54.66 Total impact

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    ABSTRACT: Bacillus subtilis CSY191, the potential probiotics and surfactin-like compound producer, was isolated from doenjang (Korean traditional fermented soybean paste).The survival rate of this strain appeared to be the 58.3% under artificial gastric conditions after 3h at pH 3.0. Surfactin was purified from the strain CSY191. Three potential surfactin isoforms were detected, with protonated masses of m/z 1030.7, 1044.7, and 1058.71. These different structures were detected in combination with Na+, K+ and Ca2+ ions by MALDI-TOF mass spectrometry. Upon 500MHz 1H NMR analysis, the surfactin isoforms had identical amino acids (GLLVDLL) and hydroxy fatty acids (of 13–15 carbons in length). The MTT assay showed that surfactin inhibited growth of MCF-7 human breast cancer cells in a dose-dependent manner, with an IC50 of approximately 10μg/ml at 24h. Additionally, the surfactin contents, during cheonggukjang fermentation with strain CSY191, increased from 0.3 to 48.2mg/kg over 48h of fermentation, while the level of anticancer activity increased from 2.6- to 5.1-fold.
    Food Chemistry 04/2012; 131(4). DOI:10.1016/j.foodchem.2011.09.133 · 3.26 Impact Factor
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    ABSTRACT: Lactobacillus brevis WCP902 that is capable of biodegrading chlorpyrifos was isolated from kimchi. The opdB gene cloned from this strain revealed 825 bp, encoding 274 aa, and an enzyme molecular weight of about 27 kDa. OpdB contains the same Gly-X-Ser-X-Gly motif found in most bacterial and eukaryotic esterase, lipase, and serine hydrolases, yet it is a novel member of the GDSVG family of esterolytic enzymes. Its conserved serine residue, Ser82, is significantly involved with enzyme activity that may have application for removing some pesticides. Optimum organophosphorus hydrolase (OpdB) activity appeared at pH 6.0 and 35 degrees C and during degradation of chlorpyrifos, coumaphos, diazinon, methylparathion, and parathion.
    Journal of Agricultural and Food Chemistry 05/2010; 58(9):5380-6. DOI:10.1021/jf903878e · 3.11 Impact Factor
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    ABSTRACT: Changes in β-glycosidase, esterase activities, isoflavone, flavanols and phenolic acid during the fermentation of Korean whole soybean fermented food cheonggukjang by Bacillus pumilus HY1 were investigated. The levels of aglycones, flavanols and gallic acid increased, while the β-glucosidase activity, esterase activity, glycosides content (except for acetylglycosides) and flavanol gallates decreased. Total isoflavone content slightly decreased after 60 h of fermentation, while total flavanol and phenolic acid content increased. The highest levels of daidzein (aglycone type) and acetyldaidzin (glycoside type) were recorded after 48 h of fermentation. The levels of catechin, epicatechin and gallic acid also increased during fermentation. However, total contents of glycosides, malonylglycosides and flavanol gallates decreased by about 80%, 90% and 60% during 60 h of fermentation, respectively. In addition, total phenolic content increased markedly during fermentation, while levels of 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical-scavenging activity increased. Hence, it would be beneficial for the food industry if components of cheonggukjang could be separated and developed into functional products.
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    ABSTRACT: We examined the role of microorganisms in the degradation of the organophosphorus (OP) insecticide chlorpyrifos (CP) during kimchi fermentation. During the fermentation of kimchi, 30 mg L(-1) of CP was added and its stability assayed during fermentation. CP was degraded rapidly until day 3 (83.3%) and degraded completely by day 9. Four CP-degrading lactic acid bacteria (LAB) were isolated from kimchi fermentation in the presence of 200 mg L(-1) CP and were identified as Leuconostoc mesenteroides WCP907, Lactobacillus brevis WCP902, Lactobacillus plantarum WCP931, and Lactobacillus sakei WCP904. CP could be utilized by these four strains as the sole source of carbon and phosphorus. Coumaphos (CM), diazinon (DZ), parathion (PT), and methylparathion (MPT) were also degraded by WCP907, WCP902, WCP931, and WCP904 when provided as sole sources of carbon and phosphorus.
    Journal of Agricultural and Food Chemistry 03/2009; 57(5):1882-9. DOI:10.1021/jf803649z · 3.11 Impact Factor
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    ABSTRACT: A new strain of Bacillus pumilus, designated HY1, was isolated from Korean soybean sauce (kanjang). This classification was based on morphological, physiological, and chemotaxonomic features of the organism that identified it as a Gram-positive bacillus, and confirmed by 16S rDNA based phylogenetic analysis. Strain HY1 showed strong antifungal activity against the aflatoxin-producing fungi Aspergillus flavus and Aspergillus parasiticus, two common contaminants of fermented soybean foods. MALDI-TOF mass analysis revealed that the antifungal compound was similar to the known lipopeptide iturin. Iturin purified from strain HY1 had three isoforms with protonated masses of m/z 1,043.4, 1,057.4, and 1,071.4, and different structures in combination with Na+ ion using MALDI-TOF MS. Purified iturin from HY1 also exhibited antifungal activity against A. flavus and A. parasiticus.
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    ABSTRACT: We developed a multiplex PCR assay for the detection of lactic acid bacteria (LAB) species, and used it to examine the LAB species involved in kimchi fermentation. The LAB profile during kimchi fermentation varied with pH and acidity. Leuconostoc mesenteroides was observed during early fermentation (pH 5.64-4.27 and acidity 0.48-0.89%), and Lactobacillus sakei become dominant later in fermentation (pH <or=4.15 and acidity >or=0.98%). The efficiency of the multiplex PCR ranged from 86.5% at day 0 (pH 6.17 and acidity 0.24%) to 100% at day 96 (pH 4.16 and acidity 1.14). This multiplex PCR assay will facilitate study of the microbial ecosystem of kimchi and its impact on kimchi fermentation.
    Molecular and Cellular Probes 12/2008; 23(2):90-4. DOI:10.1016/j.mcp.2008.12.006 · 1.87 Impact Factor
  • Food science and biotechnology 07/2008; 17(6):1240-1245. · 0.66 Impact Factor
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    ABSTRACT: Plant roots are associated with diverse communities of endophytic bacteria which do not exert adverse effects. The diversity of bacterial endophytes associated with ginseng roots cultivated in three different areas in Korea was investigated. Sixty-three colonies were isolated from the interior of ginseng roots. Phylogenetic analysis based on 16S rRNA gene sequences showed that the isolates belonged to three major phylogenetic groups: the high G+C Gram-positive bacteria (HGCGPB), low G+C Gram-positive bacteria (LGCGPB), and the Proteobacteria. The dominant species at the three different ginseng growing areas were: HGCGPB at Ganghwa (55.0%), LGCGPB at Geumsan (45.5%), and Proteobacteria at Jinan (61.9%). Most cellulase-, xylanase-, and pectinase-producing colonies among the isolates belong to the LGCGPB group, except for Pectobacterium carotovora which belonged to the Proteobacteria. The 13 isolates belonging to LGCGPB and Proteobacteria were assessed for their antifungal activity against phytopathogenic fungi such as Rhizoctonia solani. Among them, Paenibacillus polymyxa GS01, Bacillus sp. GS07, and Pseudomonas poae JA01 show potential activity as biocontrol agents against phytopathogenic fungi. Finally, most of the low G+C Gram-positive bacteria with antifungal activity against phytopathogenic microorganisms showed cellulolytic enzyme activity while some Proteobacteria with the antifungal activity and the high G+C Gram-positive bacteria did not show any cellulolytic activity.
    Microbial Ecology 09/2007; 54(2):341-51. DOI:10.1007/s00248-007-9208-3 · 3.12 Impact Factor
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    ABSTRACT: A third cel operon containing celE, celF, and celG genes was isolated from Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) genomic DNA using a cosmid library. The amino acid sequences of CelE and CelF shared high sequence identity with the cellobiose-specific PTS enzymes IIB and IIC, respectively. CelF contained the disaccharide binding region essential for acquiring cellobiose molecules. The amino acid sequence of CelG shared high sequence identity with various β-glucosidases (cellobiases) belonging to the glycosyl hydrolase family 1. Sequence and structural analysis also demonstrated that this cel operon differs from three operons previously reported from Pcc LY34, including bglTPB (accession number AY542524), ascGFB (accession number AY622309), and bglEFIA (accession number AY769096). In this study, the celF and celG genes were expressed in the presence of cellobiose. Purified CelG was estimated to be approximately 54kDa by SDS-PAGE and was able to hydrolyze salicin, arbutin, pNPG, cellobiose, and MUG, and exhibited maximal activity at pH 5.0 to 40°C. Two glutamic acid residues (Glu172 and Glu370) were shown to be essential for enzyme activity.
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    ABSTRACT: A bacterial strain Paenibacillus polymyxa GS01 was isolated from the interior of the roots of Korean cultivars of ginseng (Panax ginseng C. A. Meyer). The cel44C-man26A gene was cloned from this endophytic strain. This 4,056-bp gene encodes for a 1,352-aa protein which, based on BLAST search homologies, contains a glycosyl hydrolase family 44 (GH44) catalytic domain, a fibronectin domain type 3, a glycosyl hydrolase family 26 (GH26) catalytic domain, and a cellulose-binding module type 3. The multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities, while the enzyme domain GH26 possesses mannanase activity. The Cel44C enzyme expressed in and purified from Escherichia coli has an optimum pH of 7.0 for cellulase and lichenase activities, but is at an optimum pH of 5.0 for xylanase and mannanase activities. The optimum temperature for enzymatic activity was 50 degrees C for all substrates. No detectable enzymatic activity was detected for the Cel44C-Man26A mutants E91A and E222A. These results suggest that the amino acid residues Glu(91) and Glu(222) may play an important role in the glycosyl hydrolases activity of Cel44C-Man26A.
    Applied Microbiology and Biotechnology 01/2007; 73(3):618-30. DOI:10.1007/s00253-006-0523-2 · 3.81 Impact Factor
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    ABSTRACT: An artificial, bifunctional, thermostable cellulase-xylanase enzyme from Thermotoga maritima by gene fusion. The fusion protein exhibited both cellulase and xylanase activity when xynA was fused downstream of cel5C but no activities were shown when xynA was fused upstream of cel5C. The enzyme was optimally active at pH 5.0 and 80 degrees C over 30 min. E. coli expressed the fusion enzyme, with an apparent molecular mass of approximately 152 kDa by carboxymethyl cellulose- and xylan-SDS-PAGE.
    Biotechnology Letters 12/2006; 28(22):1857-62. DOI:10.1007/s10529-006-9166-8 · 1.74 Impact Factor
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    ABSTRACT: A third bgl operon containing bglE, bglF, bglI, and bglA was isolated from Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34). The sequences of BglE, BglF, and Bgll were similar to those of the phosphotransferase system (PTS) components IIB, IIC, and IIA respectively. BglF contains important residues for the phosphotransferase system. The amino acid sequence of BglA showed high similarity to various 6-phospho-beta-glucosidases and to a member of glycosyl hydrolase family 1. Sequence and structural analysis also revealed that these four genes were organized in a putative operon that differed from two operons previously isolated from Pcc LY34, bglTPB (accession no. AY542524) and ascGFB (accession no. AY622309). The transcription regulator for this operon was not found, and the EII complexes for PTS were encoded separately by three genes (bglE, bglF, and bglI). The BglA enzyme had a molecular weight estimated to be 57,350 Da by SDS-PAGE. The purified beta-glucosidase hydrolyzed salicin, arbutin, rhoNPG, rhoNPbetaG6P, and MUG, exhibited maximal activity at pH 7.0 and 40 degrees C, and displayed enhanced activity in the presence of Mg2+ and Ca2+. Two glutamate residues (Glu178 and Glu378) were found to be essential for enzyme activity.
    Bioscience Biotechnology and Biochemistry 05/2006; 70(4):798-807. · 1.21 Impact Factor
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    ABSTRACT: A third bgl operon containing bglE, bglF, bglI, and bglA was isolated from Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34). The sequences of BglE, BglF, and BglI were similar to those of the phosphotransferase system (PTS) components IIB, IIC, and IIA respectively. BglF contains important residues for the phosphotransferase system. The amino acid sequence of BglA showed high similarity to various 6-phospho-beta-glucosidases and to a member of glycosyl hydrolase family 1. Sequence and structural analysis also revealed that these four genes were organized in a putative operon that differed from two operons previously isolated from Pcc LY34, bglTPB (accession no. AY542524) and ascGFB (accession no. AY622309). The transcription regulator for this operon was not found, and the Ell complexes for PTS were encoded separately by three genes BglE, bglF, and bglI). The BglA enzyme had a molecular weight estimated to be 57,350 Da by SDS-PAGE. The purified beta-glucosidase hydrolyzed salicin, arbutin, rho NPG, rho NP beta G6P, and MUG, exhibited maximal activity at pH 7.0 and 40 degrees C, and displayed enhanced activity in the presence of Mg2+ and Ca2+. Two glutamate residues (Glu(178) and Glu(378)) were found to be essential for enzyme activity.
    Bioscience Biotechnology and Biochemistry 04/2006; 70(4):798-807. DOI:10.1271/bbb.70.798 · 1.21 Impact Factor
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    ABSTRACT: Pectobacterium chrysanthemi PY35 secretes the endoglucanase Cel5Z, an enzyme of the glycoside hydrolase family 5. Cel5Z is a 426 amino acid, signal peptide (SP)-containing protein composed of two domains: a large N-terminal catalytic domain (CD; 291 amino acids) and a small C-terminal cellulose binding domain (CBD; 62 amino acids). These two domains are separated by a 30 amino acid linker region (LR). A truncated cel5Z gene was constructed with the addition of a nonsense mutation that removes the C-terminal region of the protein. A truncated Cel5Z protein, consisting of 280 amino acid residues, functioned as a mature enzyme despite the absence of the SP, 11 amino acid CD, LR, and CBD region. In fact, this truncated Cel5Z protein showed an enzymatic activity 80% higher than that of full-length Cel5Z. However, cellulase activity was undetectable in mature Cel5Z proteins truncated to less than 280 amino acids.
    Applied Microbiology and Biotechnology 08/2005; 68(1):46-52. DOI:10.1007/s00253-004-1880-3 · 3.81 Impact Factor
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    ABSTRACT: An artificial bifunctional enzyme, xylanase–cellulase, has been prepared by gene fusion. Three chimeric genes were constructed that encoded fusion proteins of different lengths. The fusion proteins exhibited both xylanase (XynX) and cellulase (Cel5Z::Ω) activity when cel5Z::Ω was fused downstream of xynX, but not when xynX was fused downstream of cel5Z::Ω. Activities of bifunctional enzymes decreased when a shorter xylanase peptide was fused. Three fusion enzymes were purified, and the molecular weights of the enzymes were estimated by CMC-SDS-PAGE and XYN-SDS-PAGE to be 149, 129, and 87 kDa, respectively. The fusion enzymes displayed optimum cellulase activity at pH 8.0 and 50 °C and optimum xylanase activity at pH 8.0 and 70 °C.
    Enzyme and Microbial Technology 05/2005; DOI:10.1016/j.enzmictec.2005.01.030 · 2.97 Impact Factor
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    ABSTRACT: An asc operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) was isolated from a genomic library in a screen for beta-glucosidase activities. Sequence analysis of the 5618-bp cloned DNA fragment (accession number AY622309) showed three open reading frames (ascG, ascF, and ascB) that are predicted to encode 375, 486, and 476 amino acid proteins, respectively. The AscG ORF shared a high similarity with the Escherichia coli AscG repressor. The AscF ORF shared 81% identity with the E. coli AscF PTS enzyme II(asc), while the AscB ORF was highly similar to 6-phospho-beta-glucosidases and is a member of the glycosyl hydrolase family 1. The purified AscB enzyme hydrolyzed salicin, arbutin, pNPG, and MUG. It exhibited maximal activity at pH 7.0 and 40 degrees C, and its activity was enhanced in the presence of Mg(2+) and Ca(2+). The molecular weight of the enzyme was estimated to be 53 000 Da by SDS-PAGE. Two conserved glutamate residues (Glu(182) and Glu(374)) were shown to be important for AscB activity.
    Research in Microbiology 04/2005; 156(2):145-53. DOI:10.1016/j.resmic.2004.09.010 · 2.83 Impact Factor
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    ABSTRACT: Phylogenetic analysis of archaea in the rumen ecosystem was analysed by PCR of 16S rDNA from the bovine rumen using archaea-specific primers. The libraries were constructed from rumen fluid (AF), rumen solid (AS), and rumen epithelium (AE) from a rumen-fistulated Korean cow (Hanwoo). The 45 AF clones could be divided into three groups and the largest group was affiliated with the Methanomicrobiaceae family (96% of clones). The AF clones contained a high proportion of unidentifiable clones (67%). The 39 AE clones could be divided into two groups and the largest group was also affiliated with the Methanomicrobiaceae family (95% of clones). The AE clones contained a low proportion of unidentifiable clones (5%). The 20 AS clones could be divided into two groups that were affiliated with either the Methanobacteriaceae family (55%) or the Methanomicrobiaceae family (45%). The AS clones contained a moderate proportion of unidentifiable clones (40%). The predominant family of whole rumen archaea was found to belong to the Methanomicrobiaceae (85%). Methanomicrobiaceae were predominant in the rumen epithelium and the rumen fluid while Methanobacteriaceae were predominant in the rumen solid. One clone from the rumen fluid and two clones from the rumen epithelium contained rDNA sequences of Non-Thermophilic-Crenarchaeota (NTC) and Thermophilic-Crenarchaeota (TC), respectively, which have not previously been described from the rumen.
    Anaerobe 01/2005; 10(6):313-9. DOI:10.1016/j.anaerobe.2004.08.002 · 2.36 Impact Factor
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    ABSTRACT: A putative bgl operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) was isolated. Sequence analysis of the 5,557 bp cloned DNA fragment (accession no. AY542524) showed three open reading frames (bglT, bglP, and bglB) predicted to encode 287, 633, and 468 amino acid proteins respectively. BglT and BglP ORFs show high similarity to that of the Pectobacterium chrysanthemi ArbG antiterminator and ArbF permease respectively. Also, the latter contains most residues important for phosphotransferase activity. The amino acid sequence of BglB showed high similarity to various beta-glucosidases and is a member of glycosyl hydrolase family 1. The purified BglB enzyme hydrolyzed salicin, arbutin, pNPG, and MUG. The molecular weight of the enzyme was estimated to be 53,000 Da by SDS-PAGE. The purified beta-glucosidase exhibited maximal activity at pH 7.0 and 40 degrees C, and its activity was enhanced in the presence of Mg(2+). Two glutamate residues (Glu(173) and Glu(362)) were found to be essential for enzyme activity.
    Bioscience Biotechnology and Biochemistry 12/2004; 68(11):2270-8. · 1.21 Impact Factor
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    ABSTRACT: A putative bgl operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) was isolated. Sequence analysis of the 5,557 bp cloned DNA fragment (accession no. AY542524) showed three open reading frames (bg/T, bglP, and bglB) predicted to encode 287, 633, and 468 amino acid proteins respectively. BglT and BglP ORFs show high similarity to that of the Pectobacterium chrysanthemi ArbG antiterminator and ArbF permease respectively. Also, the latter contains most residues important for phosphotransferase activity. The amino acid sequence of BglB showed high similarity to various beta-glucosidases and is a member of glycosyl hydrolase family 1. The purified BglB enzyme hydrolyzed salicin, arbutin, pNPG, and MUG. The molecular weight of the enzyme was estimated to be 53,000Da by SDS-PAGE. The purified beta-glucosidase exhibited maximal activity at pH 7.0 and 40degreesC, and its activity was enhanced in the presence of Mg2+. Two glutamate residues (Glu(173) and Glu(362)) were found to be essential for enzyme activity.
    Bioscience Biotechnology and Biochemistry 11/2004; 68(11):2270-2278. DOI:10.1271/bbb.68.2270 · 1.21 Impact Factor
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    ABSTRACT: The composition of yeast communities in the rumen of cattle was investigated using comparativeDNA sequence analysis of yeast 26S rDNA genes. 26S rDNA libraries Were constructed front rumen fluid (FF), rumen solid (FS) and rumen epithelium (FE). A total of 97 clones, containing a partial 26S rDNA sequence of 0.6 kb length, were sequenced and Subjected to an on-line similarity search. The 41 FF Clones Could be divided into five classes. The largest class was affiliated with Pezeizomycotina class (85.4% of clones), and the remaining classes were related with the Urediniomycotina (2.4%), Hymenomycetes (4.9%), Ustilaginomycetes (4.9%) and Saccharomycotina (2.4%) classes. The 26 FE clones could be divided into three classes and the Saccharomtycetes class (92.4% of clones) was the largest group. The remaining classes were related with either Pezizomycotina (3.8%) or Ustiloginomycetes (3.8%). The 30 FS clones were all affiliated with Saccharomycotina. Saccharomycotina were predominant in rumen epithelium and rumen solid while Pezizomycotina were predominant in rumen fluid. Yeast belonging to the Saccharomycotina class was predominant in the rumen as a whole (57%). One clone (FF34) had less than 90% similarity to any sequence in the database and was thus apparently unrelated to any previously described yeast.
    The Journal of Agricultural Science 09/2004; 142:603-611. DOI:10.1017/S0021859604004708 · 2.88 Impact Factor