• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.4
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• pp.414-417
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• 1992

In order to study the addition effect of Leuconostoc mesenteroides and nisin on Escherichia coli and lactic acid bacteria during fermentation and storage of Kimchi, Kimchi was stored at 4$^{\circ}C$ for 7 days and then in-creased the temperature to $25^{\circ}C$. Lactic acid content on Kimchi fermentation at 4$^{\circ}C$ was maintained initial content which was increased upto 0.9% and lactic bacteria was also increased after switching to $25^{\circ}C$. E. coli, on the other hand, was a little decreased from the initial level, but a significant decrease was found for the those Kimchi of Leuconostoc muenteroides added and nisin treated group when the fermentation temperature was switched to $25^{\circ}C$.

• Asian-Australasian Journal of Animal Sciences
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• v.7 no.4
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• pp.505-507
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• 1994

A total of 526 domestic and experimental animals in Miyagi prefecture, Japan were investigated for fecal carriage of Campylobacter jejuni and Campylobacter coli. C. jejuni was detected in chickens (8.2%), dogs (6.3%), pigs (4.3%), cattle (1.8%) and hamsters (1.4%). C. coli was only detected from pigs (20.7%). Drug susceptibility test was performed on 5 strains of C. jejuni isolated from chickens and 13 strains of C. coli isolated from pigs to tylosin (TS), thianphenicol (TP), carbadox (CDX), chroltetracyclin (CTC), vancomycin (VCM), cefoperazone (CPZ), latamoxef (LMOX), GM were highly effective and CTC, CP and PL were moderately effective against both C. jejuni and C. coli. TS and TPH were moderately effective against C. jejuni; however, they were less effective to C. coli. One strain of C. jejuni against CTC considered to be drug resistant. The results suggest that C. jejuni and C. coli can be controlled by several drugs effectively, although a drug resistant strain exists.

• Korean journal of food and cookery science
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• v.13 no.2
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• pp.106-112
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• 1997

The effect of low concentrations of allspice (Pimenta dioica L.) in culture broth as an antibacterial agent against Escherichia coli 0157:H7 and Staphylococcus aureus 196E was tested at 35,5 and -20$^{\circ}C$. Tryptic soy broth (TSB) containing 0∼2% (w/v) of allspice was inoculated with 10$\^$5/∼10$\^$6/ cells/$m\ell$ of E. coli and S. aureus and incubated at each temperature. The growth of E. coli was not inhibited at 0.1∼1.0% allspice and growth occured at 2％ allspice but only after a prolonged lag period. Growth of S. aureus was inhibited with increasing concentration of allspice at 35$^{\circ}C$. Growth of S. aureus occured at the presence of 0.1∼0.3% allspice but the viability of S. aureus at 0.5∼2.0% allspice was decreased during storage at 35$^{\circ}C$. During refrigerated storage at 5$^{\circ}C$, inhibition of E. coli and S. aureus was increased with the progress of time and increasing spice concentration. During frozen storage at -20$^{\circ}C$, antibacterial activity of allspice against E. coli was increased with increasing storage time and spice concentration while that activity against S. aureus was effective during early period of storage. There was no major changes in population of S. aureus in TSB with different concentration of spice frozen at -20$^{\circ}C$. Viable counts of E. coli and S. aureus at 0.l％ of allspice was less than that of control during frozen storage.

• Journal of Food Hygiene and Safety
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• v.12 no.3
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• pp.200-204
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• 1997

Effects of benzoate (0~0.6 g/$\ell$ ) and sorbate (0~2.0 g/$\ell$) on the growth of Escherichia coli O157:H7 in tryptic soy broth at various pH levels (4~8) and temperatures (4$^{\circ}C$, 37$^{\circ}C$) were investigated. Benzoate and sorbate were inhibited the growth of E. coli O157:H7 up to 12 hours cultivation at 4$^{\circ}C$, and 2.0 g/$\ell$ sorbate was only inhibited during 48 hours cultivation at 37$^{\circ}C$. Among the pH levels tested, pH 4 showed significant inhibitory effect against the E. coli O157:H7 on 4$^{\circ}C$ and at 37$^{\circ}C$, respectively. When used in combination 0.2 g/$\ell$ benzoate and sorbate were completely inhibited the growth of E. coli O157:H7 on pH 4 and at 37$^{\circ}C$. While on pH 5 at 4$^{\circ}C$, all of the concentration tested did not exert any inhibitory effect. The combined effects were retarded more than single treatment of E. coli O157:H7.

• Journal of Food Hygiene and Safety
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• v.33 no.6
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• pp.495-499
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• 2018

The reduction effect of UV-C irradiation and mild heat treatment was examined against Escherichia coli O157:H7 and Salmonella Typhimurium on black pepper powder. E. coli O157:H7 (ATCC 35150) and S. Typhimurium (ATCC 19585) were inoculated onto black pepper powder at approximately $10^7$ and $10^6CFU/g$, respectively. E. coli O157:H7 and S. Typhimurium were treated with UV-C and mild heat at $60^{\circ}C$. A UV-C intensity ($2.32W/cm^2$ ) was used for 10 min to 70 min at $60^{\circ}C$. After UV-C and heat treatment at $60^{\circ}C$, microbial analysis and color change of black pepper powder was conducted. E. coli O157:H7 and S. Typhimurium were reduced by a level of 1.89 and 2.24 log CFU/g, respectively, when treated with UV-C alone for 70 min. And E. coli O157:H7 and S. Typhimurium were reduced by 2.22 and 5.10 log CFU/g, respectively, when treated with mild heat treatment at $60^{\circ}C$ alone for 70 min. But when combined with UV-C and mild heat, it showed higher levels of reduction by 2.46 and 5.70 log CFU/g. S. Typhimurium was more easily reduced than E. coli O157:H7. Color values were not significantly (p > 0.05) different in all treated samples. Therefore, these results suggest that the combined treatment with UV-C and mild heat was effective to inactivate the food pathogens in black pepper powder and can be used as a food industrial microbial intervention method.

• Journal of Microbiology and Biotechnology
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• v.23 no.12
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• pp.1726-1736
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• 2013

Biosynthesis of indole-3-acetic acid (IAA) via the indole-3-pyruvic acid pathway involves three kinds of enzymes; aminotransferase encoded by aspC, indole-3-pyruvic acid decarboxylase encoded by ipdC, and indole-3-acetic acid dehydrogenase encoded by iad1. The ipdC from Enterobacter cloacae ATCC 13047, aspC from Escherichia coli, and iad1 from Ustilago maydis were cloned and expressed under the control of the tac and sod promoters in E. coli. According to SDS-PAGE and enzyme activity, IpdC and Iad1 showed good expression under the control of $P_{tac}$, whereas AspC was efficiently expressed by $P_{sod}$ originating from Corynebacterium glutamicum. The activities of IpdC, AspC, and Iad1 from the crude extracts of recombinant E. coli Top 10 were 215.6, 5.7, and 272.1 nmol/min/mg-protein, respectively. The recombinant E. coli $DH5{\alpha}$ expressing IpdC, AspC, and Iad1 produced about 1.1 g/l of IAA and 0.13 g/l of tryptophol (TOL) after 48 h of cultivation in LB medium with 2 g/l tryptophan. To improve IAA production, a tnaA gene mediating indole formation from tryptophan was deleted. As a result, E. coli IAA68 with expression of the three genes produced 1.8 g/l of IAA, which is a 1.6-fold increase compared with wild-type $DH5{\alpha}$ harboring the same plasmids. Moreover, the complete conversion of tryptophan to IAA was achieved by E. coli IAA68. Finally, E. coli IAA68 produced 3.0 g/l of IAA after 24 h cultivation in LB medium supplemented with 4 g/l of tryptophan.

• Korean Journal of Microbiology
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• v.32 no.1
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• pp.47-52
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• 1994

The cells of Campylobacter jejuni heat-shocked at 48${\circ}C$ for 30 min synthesized the heat shock proteins of HSP90, HSP66 and HSP60. Those heat shock proteins were found to correspond to the heat shock proteins of HSP87, HSP66 (DnaK), and HSP58 (GroEL) of E. coli, respectively. By Southern blot analysis of the chromosomal DNAs of C. jejuni with groESL and dnaK genes of E. coli as DNA probes, the heat shock genes of C. jejuni which are homologous to the E. coli groESL and dnaK genes were found to exist in the chromosomal DNA. The genomic libraries of C. jejuni were constructed with the cosmid vector pWE15 and the groEL gene of C. jejuni were cloned in E. coli B178 groEL44 temperature senstive mutant. The hybrid plasmid (pLC1) was inserted with the DNA fragment (about 5.7kb in size) containing the groEL gene. E. coli groEL44 mutant cell transformed with the pLC1 could grow at 42${\circ}C$ by synthesizing the HSP60 of C. jejuni and regained the susceptibility to the ${\lambda}$ vir phage by expression of the groEL gene in the cloned cells. These indicated that the groEL products of C. jejuni had chaperon effects by synthesizing the heat shock proteins in the cloned cells of E. coli.

• BMB Reports
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• v.29 no.2
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• pp.116-121
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• 1996

In earlier studies, the genes encoding Escherichia coli thioredoxin and Corynebacterium nephridii thioredoxin C-3 were fused via a common restriction site in the nucleotide sequence coding for the active site of the proteins to generate two chimeric thioredoxins, designated E-C3 (N to C-terminal) and C3-E. The hybrid thioredoxins were overexpressed in E. coli from the cloned chimeric thioredoxin genes by a T7 promoter/polymerase system. To investigate the structure-function relationship of thioredoxin, we purified the E-C3 hybrid thioredoxin through ammonium sulfate fractionation, DEAE-cellulose chromatography, and Sephadex G-50 gel filtration. Its purity was examined on SDS-polyacrylamide gel electrophoresis and the molecular weight of the purified E-C3 hybrid thioredoxin was estimated to be 12,000. On native polyacrylamide gels, the purified E-C3 hybrid thioredoxin shows a much lower mobility than E. coli thioredoxin. E-C3 hybrid thioredoxin exhibits a 40-fold lower catalytic efficiency with E. coli thioredoxin reductase than E. coli thioredoxin. It was shown to catalyze the reduction of insulin disulfide by dithiothreitol. The purified E-C3 hybrid thioredoxin was also characterized in other aspects.

• Microbiology and Biotechnology Letters
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• v.32 no.3
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• pp.212-217
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• 2004

The gene coding for mannanase from Bacillus subtilis WL-7, a number of glycosyl hydrolase family 26, was hyperexpressed in Escherichia coli. Two recombinant plasmids, pE7MAN and pENS7, were constructed by introducing the complete mannanase gene and the mature mannanase gene lacking N-terminal signal peptide region into a expression vector pET24a(＋), respectively. The level of mannanase produced by E. coli BL21 (DE3) carrying pENS7, which included the mature mannanase gene, was considerably higher than that by E. coli BL21 (DE3)/pE7MAN. Almost mannanase produced by the recombinant E. coli carrying pENS7 at growth temperature of $37^{\circ}C$ existed as inactive enzyme of insoluble form. Growth at temperature below $31^{\circ}C$ increased the soluble fraction of mannanase having catalytic activity in the recombinant E. coli cells. The highest productivity of active mannanase was observed in cell-free extract of the recombinant E. coli grown at growth temperature ranging from $25^{\circ}C$ to $28^{\circ}C$, while mannanase activity per soluble protein of the cell-free extract was highest in the cells grown at $^31{\circ}C$.

• Journal of Life Science
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• v.28 no.2
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• pp.257-264
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• 2018

The YrdC superfamily is a group of proteins that are highly conserved in almost all organisms sequenced so far. YrdC in Escherichia coli was suggested to be involved in ribosome biogenesis, translation termination, cold adaptation, and threonylcarbamoyl adenosine formation in tRNA. In this study, to unambiguously demonstrate that yrdC is essential in E. coli, we constructed two yrdC mutant strains of E. coli and examined their phenotypes. In the temperature-sensitive yrdC mutant strain, cell growth stopped almost immediately under nonpermissive conditions and it appeared to accumulate 16S ribosomal RNA precursors without significant accumulation of 30S ribosomal subunits. We also cloned yeast and human homologs and demonstrated that they complement the E. coli yrdC-deletion strain. By mutational study, we demonstrated that the concave surface in the middle of the YrdC protein plays an important role in E. coli, yeast, and human versions. By comparison of two yrdC-deletion strains, we also unambiguously demonstrated that yrdC is essential for viability in E. coli and that the functions of its yeast and human homologs overlap with that of E. coli YrdC.