• Applied Biological Chemistry
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• v.33 no.4
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• pp.343-348
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• 1990

E. coli LE392, transformed with CDDP-treated pBR322 DNA, was plated on ampicillin containing media. The number of colonies formed on ampicillin containing agar plate was reduced to undetectable level after treat the DNA with 13.3 ${\mu}M$ CDDP. The CDDP-treated pBR322 DNA was susceptible to sing1e strand DNA specific S1 nuclease and it's migration Pattern in agarose gel electrophoresis was changed. These results suggest that CDDP adduction to pBR322 DNA resulted in denaturation of the double helix and changes in it's conformation which ultimately leads In the inactivation of the ampicillin resistant sere.

• YAKHAK HOEJI
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• v.3 no.1
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• pp.4-9
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• 1957

Effects of antibioties on micro-organism have been reported by many scientists, such as Krampitz and Werkman, Fisher, Gale and Rodwell, Klimick Cavalito and Bailey, Umbreit, etc. On the mechanism by which penicillin act, Fisher(1947), Platt(1947), and Cavallito, considered that penicillin might act on bacteria by inhibiting with the normal function of SH-group of glutathione in the metabolism of the cell. Resenbrance of penicillin to gultathione in structure and the inactivation of penicillin by cysteine make us approve of the above inhibiting theory of SH-group. Galland (1947) and Schmidt (1947) reported that penicillin inhibited the activity of ribonuclease, Phosphatase, and mononucleotidase. Gale (1948) discovered that the gram positive bacteria had lost the power to uptake glutamic acid by ribonucleic acid in the medium contained penicillin: growth of gram positive organism was inhibited by the results that penicillin inhibited the uptake of amino acid byribonucleic acid, acting on ribonucleic acid of gram positive bacteria. Hotchkiss (1950) cultured S. aureus in the medium contained glucose and amino acids, and studied the effect of penicillin on protein synthesis. Peptide formation in living cells was inhibited by penicillin, while amono acid was utilized as before the addition of penicillin. On the otherhand, Binkley (1951) found penicillin interfered hydrolase of glutath one, and Hans (1950) reported penicillin inhibited the transpeptidation. On the machanism by which streptomycin acts. Cohen (1947) reported steptomycin made a irreversible complex with desoxyribonucleic acid, by the fact that desoxyribonucleic acid formed the precipitates with diguanide group of steptomycin. Zeller (1951) reported, on the other hand, streptomycin inhibited diamine oxidease. Geiger (1947) and Umbreit (1949) reported that steptomycin inhibited condensation of oxaloacetate and pyruvate in E. Coli and Oginsky et al (1949) reported steptomycin inhibited oxaloacetate-pyruvate reaction in Kreb's cycle. On the mechanism by which terramycin acts, Hahn & Wisseman (1951) reported that the formation of adaptive enzyme was inhibited by terramycin in E. Coli cultivated in the medium contained loctose, and that the protein synthesis was inhibited by terramycin. However, effects of antibiotics on amino acid metabolism have not been discussed much in spite of its important role in living cells. Especislly, effects of anitibiotics on higher plants have scarcely been reported. Here, to prove the effect of antibiotics on higher plants, and the mechanism by which, through amino acid metabolism, they promote or inhibit growth of plants, amino acids in bean plants treated with penicillin, streptomycin, and terramycin were analyzed by paper chromatography. And to clarify the antagonis of cysteine (as SH-group) against penicillin, through amino acid metabolism, amino acids in bean plants treated with cystene and penicillin, at the same time, were also analyzed.

• Korean Journal of Veterinary Service
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• v.44 no.3
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• pp.149-155
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• 2021

In virucidal efficacy testing, the chemical inactivation cannot be determined for all viruses due to the difficulties or the inability to culture sufficiently or the risk of exposure to the viruses. Therefore, disinfectants against these viruses could be evaluated by different methods and surrogate viruses are used as alternative. In this study we developed a method for efficacy testing of veterinary disinfectants using one of the candidate surrogate viruses, bacteriophage MS2, as part of the research on the selection of surrogate viruses for efficiency of efficacy testing of veterinary disinfectants. This method is based on the Animal and Plant Quarantine Agency (APQA) guidelines for efficacy testing of veterinary disinfectants. Bacteriophage and disinfectant are reacted in suspension in accordance with the APQA guidelines and then a newly established double agar layer method is applied for the efficacy test. The double agar layer method is summarized as follows: 1) The bottom agar with 1.5% agar is boiled and cooled before poured into petri dishes at volume of 20 mL, and dried under biological safety cabinet. 2) The top agar with 0.7% agar is boiled and kept at 50℃ before E. coli culture was seeded. 3) The serially diluted bacteriophage MS2-disinfectant mixtures 0.05 mL and E. coli host 0.01 mL (OD₆₀₀ 0.2~0.3) are mixed with 5 mL of top agar and incubate them at 50℃ for 5 min for reaction. 4) The resulting mixture is poured over top of a bottom agar plate and rocked sufficiently to ensure that the top agar covers the entire surface of the bottom agar. 5) The double agar layer is then placed under biological safety cabinet to allow the agar layer to solidify and subsequently incubated at 37℃ for 24 hr. 6) Following incubation, the plates may be inspected for plaques and record results.

• Microbiology and Biotechnology Letters
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• v.26 no.6
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• pp.483-489
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• 1998

We carried out the expression and characterization of yeast thioredoxin system including thioredexin 1 (Trx1), Trx2, thioredoxin reductase (TR), and a novel thioredoxin (Trx3), which was reported in the data base of Saccharomyces genome. The Trx1, 2 and TR were expressed as soluble proteins in E. coli and the sizes of purified proteins were equal to the reported their molecular weights. The expressed Trx3 was found in both soluble fraction and precipitate. The size of Trx3 purified from soluble fraction of E. coli crude extracts was estimated as 14 kDa on SDS-PAGE instead of 18 kDa for Trx3 in precipitate. N-terminal amino acid sequence of the small size of purified Trx3 from soluble fraction was analyzed as FQSSYTS which is correspond to the sequence from 20 to 26 for Trx3. Trx3 together with thioredoxin reductase and NADPH was able to reduce the disulfide bridge of insulin and 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). Trx3 stimulated the antioxidant effect of thioredoxin peroxidase 1 (TPx1) which inhibited inactivation of glutamine synthetase (GS) in dithiothreitol (DTT) containing metal catalyzed oxidation system. The stimulation effect of Trx3 was 10% of the effect of either Trx1 or Trx2. In addition, Trx3 could reduce the disulfide of TPx to thiol, so that the TPx had thioredoxin dependant peroxidase activity. In western blotting analysis, antibodies against purified Trx3 did not cross-react with crude extracts of yeast, purified Trx1, and Trx2 proteins. But, in PCR reaction using the cDNA library of yeast as a template, gene encoding of trx3 was amplified.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.5
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• pp.765-769
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• 2002

Improvement of hygienic quality of powdered raw grains and vegetables by fermentation was investigated. Luc-tobacillus sp. isolated from kimchi was used as a starter. The cell counts of coliform group and SS enteric bacteria on the SS agar plate in raw grains and vegetables were 2.3$\times$103 cfu/mL and 8.6$\times$10$^3$ cfu/mL, respectively. The starlet, Lactobacillu sp., reached 10$^{7}$ cfu/mL after 48 hr in fermentation. At that time, the coliform group and enteric bacteria on the SS agar plate were gradually inactivated and eliminated after 60 hr of fermentation. During the fermentation process, pH of the suspension was lowered and acidity increased. Antimicrobial activity of the acidic supernatant of fermented raw grains and vegetal]les against the E. coli sp. and Salmonella sp. was higher than that of lactic acid solution or neutralized supernatant. Therefore, it was considered that antimicrobial effect of the fermented raw grains and vegetal]les might be accelerated by tile synergic effect of acid and bacteriocin, and liquid fermentation of powdered raw grains and vegetables will be effective for inactivation of hygienic microorganisms.

• Korean Journal of Food Science and Technology
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• v.45 no.4
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• pp.495-500
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• 2013

This study was performed to identify safe natural food preservatives from medicinal herbs and to evaluate the antimicrobial effects of medicinal plants against microorganisms. Medicinal herbs were extracted 3 times with methanol at $45^{\circ}C$ for 3 h and fractionated with n-hexane. The antimicrobial effects of the fractions were determined by measuring the diameter of the inhibition zone by using an agar-well diffusion assay. The MIC of fractions for the inhibition of microorganisms was determined using a microplate reader. The antimicrobial effects of fractions were greater against gram positive bacteria than against gram negative bacteria, but the difference was not significant. The antimicrobial effects of fractions were concentration dependent. While these results have implications, the underlying mechanisms of microbial inactivation need to be further elucidated. The results showed the possibility of developing safer food preservatives.

• Food Science of Animal Resources
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• v.35 no.3
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• pp.406-412
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• 2015

The combined effects of electron-beam irradiation and ageing of beef were examined. The irradiated samples at dose of 0 or 2 kGy were kept and analyzed for the microbial growth, shear values, meat color, and nucleotide-related flavor compounds at different ageing temperatures (2, 10, or 25℃) for 8 d. The irradiation effect on inactivation of foodborne pathogens was also investigated. The population of Listeria monocytogenes and E. coli O157:H7 inoculated in beef samples decreased in proportion to the irradiation dose, showing D₁₀ values of 0.66 and 0.65 kGy respectively. The irradiated beef eye of round had lower number of total aerobic bacteria (TAB) than nonirradiated one during the storage, but the TAB increased with higher ageing temperature (p<0.05). Especially, TAB increased sharply in non-irradiated samples aged at 25℃ after 4 d (p<0.05). With increasing ageing temperature and ageing time, shear force values decreased (p<0.05). The color a* values of the irradiated beef were lower than those of the non-irradiated throughout the ageing period (p<0.05). As ageing time and temperature increased, the amounts of inosine monophosphate decreased and the hypoxanthine increased (p<0.05). Relatively high ageing temperature could be used at irradiated beef eye of round to shorten the ageing time.

• Journal of Microbiology and Biotechnology
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• v.17 no.3
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• pp.454-460
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• 2007

Enzymatic properties and substrate specificity of recombinant $\beta-glycosidases$ from a hyperthermophilic archaeon, Sulfolobus shibatae (rSSG), were analyzed. rSSG showed its optimum temperature and pH at $95^{\circ}C$ and pH 5.0, respectively. Thermal inactivation of rSSG showed that its half-life of enzymatic activity at $75^{\circ}C$ was 15 h whereas it drastically decreased to 3.9 min at $95^{\circ}C$. The addition of 10 mM of $MnCl_2$ enhanced the hydrolysis activity of rSSG up to 23% whereas most metal ions did not show any considerable effect. Dithiothreitol (DTT) and 2-mercaptoethanol exhibited significant influence on the increase of the hydrolysis activity of rSSG rSSG apparently preferred laminaribiose $(\beta1\rightarrow3Glc)$, followed by sophorose $(\beta1\rightarrow2Glc)$, gentiobiose $(\beta1\rightarrow6Glc)$, and cellobiose $(\beta1\rightarrow4Glc)$. Various. intermolecular transfer products were formed by rSSG in the lactose reaction, indicating that rSSG prefers lactose as a good acceptor as well as a donor. The strong intermolecular transglycosylation activity of rSSG can be applied in making functional oligosaccharides.

• Journal of the Semiconductor & Display Technology
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• v.23 no.1
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• pp.84-87
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• 2024

A water sterilization system is developed utilizing a 275 nm-wavelength LED light source equipped with a TIR lens. The system's light source is constructed by combining a 275 nm-wavelength UVC LED, known for its germicidal properties, with a TIR lens having a direction angle of 6.8 degrees. The optical simulation software 'LightTools' is employed to design and optimize the intensity of deep ultraviolet sterilizing light irradiation, its distribution, and sterilization capacity. In the inactivation experiment with E. coli, the water sterilizer system achieved a sterilization rate of 78.92 % while maintaining a water flow capacity of 50 L/min. Compared to the conventional mercury lamp light source water sterilizer system, the UVC LED water sterilizer system addresses environmental concerns related to mercury usage and offers advantages in terms of lifespan and durability.

• Journal of Microbiology
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• v.35 no.4
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• pp.300-308
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• 1997

The catechol 2,3-dioxygenase (C23O) encoded by the Pseudomonas putida xylE gene was over-produced in Escherichia coli and purified to homogeneity. The activity of the C23O required the reduced form of the Fe(II) ion since the enzyme was highly susceptible to inactivation with hydrogen perocide but reactivated with the addition of ferrous sulfate in conjunction with ascorbic acid. The C23O activity was abolished by treatment with the chemical reagents, diethyl-pyrocarbonate (DEPC), tetranitromethane (TNM), and 1-cyclohexy1-3-(2-morpholinoethyl) car-bodiimidemetho-ρ-toluenesulfontate (CMC), which are modifying reagents of histidine, tyrosine and glutamic acid, respectively. These results suggest that histidine, tyrosine and glutamic acid residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues among several extradion dioxygenases and have the chemical potential to serveas ligands for Fe(II) coordination. Analysis of random point mutants in the C23O gene derived by PCR technique revealed that the mutated positions of two mutants, T179S and S211R, were located near the conserved His165 amd Hos217 residues, respectively. This finding indicates that these two positions, along with the conserved histidine residues, are specially effective regions for the enzyme function.