Manuka honey (MH) has been shown anti-bacterial activity against several pathogenic bacteria. However, the inhibitory effect of MH on biofilm formation by Escherichia coli O157:H7 has not yet been examined. In this study, MH significantly reduced E. coli O157:H7 biofilm. Moreover, pre- and post-treatment with MH also significantly reduced E. coli O157:H7 biofilm. Cellular metabolic activities exhibited that the viability of E. coli O157:H7 biofilm cells was reduced in the presence of MH. Further, colony forming unit of MH-treated E. coli O157:H7 biofilm was significantly reduced by over 70%. Collectively, this study suggests the potential of anti-biofilm properties of MH which could be applied to control E. coli O157:H7.
Reaction of arachno-S2B7H8- with either THF or 1,2-dimethoxyethane upon refluxing condition results in the formation of the previously known compound hypho-S2B7H10-. Protonation of hypho-S2B7H10- with HCl/Et2O generates hypho-2,5-S2B7H11 in good yield. This hypho-S2B7H10- anion has been employed to generate a series of new nido-, arachno-, and hypho-metalladithiaborane clusters. Reaction of the anion with Cp(CO)2FeCl results in direct metal insertion and the formation of a complex containing the general formula (η5-C5H5)FeS2B7H8. Spectroscopic studies of nido-6-CpFe-7,9-S2B7H8 Ⅰ demonstrated that compound Ⅰ was shown to have an nido-type cage geometry derived from an octadecahedron missing one vertex, with the iron atom occupying the three-coordinate 6-position in the cage and the two sulfurs occupying positions on the open face of the cage. Reaction of hypho-S2B7H10- with CoCl2/Li+[C5H5]- gave the previously known complex arachno-7-CpCo-6,8-S2B6H8 Ⅱ. Also, the reaction of the anion with [Cp*RhCl2]2 gave the complex arachno-7-Cp*Rh-6,8-S2B6H8 Ⅲ, the structure of which was shown to be that of complex Ⅱ. The similarity of the NMR spectra of Ⅱ and Ⅲ suggest that Ⅲ adopts cage structure similar to that previously confirmed for Ⅱ. A series of 9-vertex hypho clusters in which the sulfur atoms are bridged by different species isoelectronic with a BH3 unit, such as HMn(CO)4 or SiR2 have been prepared. Compounds Ⅳ,Ⅴ and Ⅵ are each 2n+4 skeletal electron systems and would be expected according to skeletal electron counting theory to adopt hypho-type polyhedral structures derived from an icosahedron missing three vertices. The complex hypho-1-(CO)4Mn-2,5-S2B6H9 Ⅳ was obtained by the reaction of the anion with (CO)5MnBr and has been shown from spectroscopic data to consist of a (CO)4Mn fragment bound to the two sulfur atoms S2 and S5 of hypho-S2B7H10-. Also, similar hypho-type complexes hypho-1-R2Si-2,5-S2B6H8 (R=CH3 Ⅴ, R=C6H5 Ⅵ) have been prepared from the reaction of hypho-S2B7H10- with R2SiHCl.
Recently, sporadic cases of human infection by genetic reassortants of H7Nx influenza A viruses have been reported; such viruses have also been continuously isolated from avian species. In this study, A/wild bird/South Korea/sw-anu/2023, a novel reassortant of the H7N1 avian influenza virus, was analyzed using full-genome sequencing and molecular characterization. Phylogenetic analysis showed that A/wild bird/South Korea/sw-anu/2023 belonged to the Eurasian lineage of H7Nx viruses. The polymerase basic (PB)2, PB1, polymerase acidic (PA), and nucleoprotein (NP) genes of these viruses were found to be closely related to those of avian influenza viruses isolated from wild birds, while the hemagglutinin (HA), neuraminidase (NA), matrix (M), and nonstructural (NS) genes were similar to those of avian influenza viruses isolated from domestic ducks. In addition, A/wild bird/South Korea/sw-anu/2023 also had a high binding preference for avian-specific glycans in the solid-phase direct binding assay. These results suggest the presence of a new generation of H7N1 avian influenza viruses in wild birds and highlight the reassortment of avian influenza viruses found along the East Asian-Australasian flyway. Overall, H7Nx viruses circulate worldwide, and mutated H7N1 avian viruses may infect humans, which emphasizes the requirement for continued surveillance of the H7N1 avian influenza virus in wild birds and poultry.
Objectives : The aim of this study was to investigate the effect of baicalein (BA) on the production of hydrogen peroxide and nitric oxide (NO) in RAW 264.7 mouse macrophages stimulated with polyinosinic-polycytidylic acid (poly-IC) and lipoteichoic acid. Methods : RAW 264.7 co-stimulated with poly-IC and lipoteichoic acid were incubated with baicalein at concentrations of 25 and 50 μM. Incubation time is 16 h, 18 h, 20 h, 22 h, and 24 h. After incubation, The production of hydrogen peroxide in RAW 264.7 was measured with dihydrorhodamine 123 assay. Chrysin was used as a comparative material. NO production was evaluated by griess assay. Results : For 16 h, 18 h, 20 h, 22 h, and 24 h incubation, BA at the concentration of 25 and 50 μM significantly inhibited the production of hydrogen peroxide in RAW 264.7 stimulated by poly-IC and lipoteichoic acid (p <0.001). In details, production of hydrogen peroxide in 'poly-IC and lipoteichoic acid'-stimulated RAW 264.7 treated for 16 h with BA at concentrations of 25 and 50 μM was 82.36% and 77.24% of the control group treated with poly-IC and lipoteichoic acid only, respectively; the production of hydrogen peroxide for 18 h was 83.15% and 77.91%, respectively;production of hydrogen peroxide for 20 h was 82.88% and 77.82%, respectively; production of hydrogen peroxide for 22 h was 83.27% and 78.17%, respectively; production of hydrogen peroxide for 24 h was 83.54% and 78.35%, respectively. Additionally, BA at the concentration of 50 and 100 μM significantly inhibited NO production in lipoteichoic acid-induced RAW 264.7 (p <0.001). Conclusions : BA might have anti-oxidative activity related to its inhibition of hydrogen peroxide production in 'poly-IC and lipoteichoic acid'-stimulated RAW 264.7 macrophages.
B7-H4 is a member of B7 family of co-inhibitory molecules and B7-H4 protein is found to be overexpressed in many human cancers and which is usually associated with poor survival. In this study, we developed a therapeutic vaccine made from a fusion protein composed of a tetanus toxoid (TT) T-helper cell epitope and human B7-H4IgV domain (TT-rhB7-H4IgV). We investigated the anti-tumor effect of the TT-rhB7-H4IgV vaccine in BALB/c mice and SP2/0 myeloma growth was significantly suppressed in mice. The TT-rhB7-H4IgV vaccine induced high-titer specific antibodies in mice. Further, the antibodies induced by TT-rhB7-H4IgV vaccine were capable of depleting SP2/0 cells through complement-dependent cytotoxicity (CDC) in vitro. On the other hand, the poor cellular immune response was irrelevant to the therapeutic efficacy. These results indicate that the recombinant TT-rhB7-H4IgV vaccine might be a useful candidate of immunotherapy for the treatment of some tumors associated with abnormal expression of B7-H4.
Shampoos are used routinely by a large number of veterinarians to treat skin diseases. Skin pH is affected by shampoos, however, known to occur. In order to evaluate the effect of shampoos on skin surface pH, we performed the measurement of skin pH using skin pH meter PH900 in five healthy mixed breed dogs. The seven commercial shampoos: Humilac, Sebocalm, Sebolytics, Etiderm, PEroxyderm, HyLyt and Zn-7 Derm were included in this study. The anatomical sites, right thorax was the highest pH (7.66$\pm$0.10), and the lowest pH (6.20$\pm$0.23) was left pinna. A statiscally significant decrease in skin pH was found 7 minutes after application of Humilac, Sebocalm, Etiderm, Peroxyderm (p<0.01) and Sebolytics (p<0.05). After 17 minutes of application skin surface pH was inclined to increase in every shampoos but the degree of increase was slight at 77 minutes. No statiscally significant differences were found in HyLy-T and Zn-7 Derm, but skin pH was normal range (6.2-7.8) after application. Throughout the experiment skin surface pH was maintained above pH 7.0 in detergent. The commercial shampoos, Humilac, Sebocalm, Etiderm, had the decreasing effect on skin surface pH in dogs. The other four shampoos maintain the skin pH normal range. The skin pH meter PH 900 was found simple and useful for skin pH measurement.
Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.
This study was performed to investigate the synergistic effect of chitosan and sorbic acid as a new food preservative. So it was performed to investigate inhibitory effect on growh of E. coli 0157:H7, gram negative pathogenic food borne disease bacteria and of S. aureus, gram positive food borne disease bacteria in chitosan, sorbic acid and combination of chitosan and sorbic acid. Minimun Inhibitory Concentration (MIC) of chitosan in E. coli 0157:H7 was 500 ppm at pH 5.0, 250 ppm at pH 5.5, 500 ppm at pH 6.0, and 2000 ppm at pH 6.5, while in Staph. aureus 31.25 ppm at pH 5.0 and 62. 5 ppm at more than pH 5.5. also, MIC of sorbic acid in E. coli 0157:H7 was 500 ppm at pH 5.0, 1500 ppm at pH 5.5, and 2000 ppm at more than pH 6.0, while in Staph. aureus 1500 ppm at pH 5.0 and more than 2000 ppm at more than pH 5.5. Due to the effect of pH in E. coli 0157:H7, MIC of combined chitosan and sorbic acid was 500 ppm of chitosan with 500 ppm of sorbic acid at pH 6.5, but 250 ppm of chitosan with 31.3 ppm of sorbic acid at pH 5.0. In Staph. aureus, there was great effect of chitosan, but neither effect of pH nor sorbic acid. When E. coli 0157:H7 were treated with 500 ppm of chitosan with 500 ppm of sorbic acid and 250 ppm of chitosan with 250 ppm of sorbic acid at pH 6.5, they were inhibited. But, they were increased at the initial concentration of bacteria at 1000 ppm of chitosan in 18 hours, at 500 ppm of chitosan in 36 hours. There was no effect of growth inhibition with sorbic acid but great effect with chitosan on Staph. aureus. The correl~tions between MICs of chitosan and sorbic acid in E. coli 0157:H7 accoding to pH were higher than those in Staph. aureus. R values in E. coli 0157:H7 were 0.95 (p<0.01), 0.99 (p<0.01), 0.97 (p<0.01), and 0.99 (p<0.01) at pH 6.5, 6.0, 5.5, and 5.0 respectively. The synergistic effect of chitosan and sorbic acid in E. coli 0157:H7 could be confirmed from the result of this experiment. Therefore, it was expected that the food preservation would increase or maintain by using sorble acid together with chitosan, natural food additive that did no harm to human body.
This study was conducted to investigate the functionality of soybean protein isolates extracted in acidic range (pH 2.0 and 3.0), neutral range (pH 7.0) and alkaline range (pH 10.0 and 12.0). The protein content of soybean protein isolates extracted at pH 3.0 was maximum (93.31%), but that of pH 7.0 was minimum (73.93%). The extraction yield of soybean protein isolates extracted at pH 3.0 was minimum (0.36%), but that of pH 12.0 was maximum (47.54%). The functionality (solubility, water absorption, oil absorption, foam capacity, foam stability, emulsion capacity and gelation) of soybean protein isolates was significantly influenced by pH of extraction medium. The soybean protein isolates extracted at pH 2.0 and 3.0 were more soluble at acidic ranges and those of pH 3.0 and 7.0 were more soluble at neutral ranges, but those of pH 2.0, 3.0, 7.0, 10.0 and 12.0 were more soluble at alkaline ranges than other ranges. The soybean protein isolates extracted at pH 2.0 and pH 12.0 gave greater water absorption, oil absorption and foam capacity than those extracted at pH 3.0, pH 7.0 and pH 10.0. And the emulsion capacity of soybean protein isolates was increased by the increase of extraction pH.
This study calculated kinetic parameters of Escherichia coli O157:H7 and developed a probabilistic model to estimate growth probabilities of E. coli O157:H7 on polyethylene cutting boards as a function of temperature and time. The surfaces of polyethylene coupons ($3{\times}5$ cm) were inoculated with E. coli O157:H7 NCCP11142 at 4 Log $CFU/cm^2$. The coupons were stored at 13 to $35^{\circ}C$ for 12 h, and cell counts of E. coli O157:H7 were enumerated on McConkey II with sorbitol agar every 2 h. Kinetic parameters (maximum specific growth rate, Log $CFU/cm^2/h$; lag phase duration, h; lower asymptote, Log $CFU/cm^2$; upper asymptote, Log $CFU/cm^2$) were calculated with the modified Gompertz model. Of 56 combinations (temperature${\times}$time), the combinations that had ${\geq}$0.5 Log $CFU/cm^2$ of bacterial growth were designated with the value of 1, and the combinations that had increases of <0.5 Log $CFU/cm^2$ were given the value 0. These growth response data were fitted to the logistic regression to develop the model predicting probabilities of E. coli O157:H7 growth. Specific growth rate and growth data showed that E. coli O157:H7 cells were grown at $28-35^{\circ}C$, but there were no obvious growth of the pathogen below $25^{\circ}C$. Moreover, the developed probabilistic model showed acceptable performance to calculate growth probability of E. coli O157:H7. Therefore, the results should be useful in determining upper limits of working temperature and time, inhibiting E. coli O157:H7 growth on polyethylene cutting board.
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