• Korean Journal of Veterinary Research
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• v.44 no.3
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• pp.441-448
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• 2004

DNase activity in Haemonchus contortus reproductive tissue was characterized and compared to that in whole worm. DNase activity in reproductive tissue was detected throughout pHs 4-10 with high activity under acidic conditions. The activity was not inhibited by 10 mM EDTA at pH 5.0, but largely inhibited by pH 7.0. The activity produced DNA fragments with mixtures of 3'-hydroxyls (OH) and 3'- phosphates (P) at each pH. Three distinct DNase activities were identified and had $M_rs$ of 34, 36 and 38.5 kDa in zymograms, which were distinguished according to pH requirement and sensitivity to EDTA. Among them, the 36 kDa reproductive tissue DNase had predominant activity at pH 5.0, but very weak at pH 7.0, and this activity was not inhibited by EDTA at pH 5.0. These characteristics of the 36 kDa reproductive tissue DNase resemble those of classic acidic DNases. In contrast, 36 kDa whole worm DNase activity had high activity at both pH 5.0 and 7.0. While the 36 kDa DNase activity at pH 5.0 was similar in both reproductive tissue and whole worm samples, the activity at pH 7.0 was predominantly detected in whole worm sample. This suggests that the 36 kDa whole worm DNase at pH 5.0 differs from that at pH 7.0. Thus, results indicate that the EDTA-insensitive 36 kDa DNase at pH 5.0 is specific for H. contortus reproductive tissue.

• Journal of the Institute of Electronics and Information Engineers
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• v.52 no.3
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• pp.199-205
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• 2015

This study is about ionic water generator filter Recently, a lot of people feel deep interest in health and drinking water. And there are various types of water. Ionic water generator is a system with special function, and can be classified as a medical device and should be manufactured after approval from the Food and Drug Administration. Basically ionized water is different from the packaged and stored water. When the tap water or ground water passes through the various filters of ionic water generator, it turns to the purified water of pH7 ~ 7.5 and we can electrolyze that water into anion and cation by diaphragm. And in negative electrode side, we can get alkaline water with calcium ($Ca^+$), potassium ($K^+$), magnesium ($Mg^+$), sodium ($Na^+$) for body. In general, we can change pH value from 5 to 9 of ionizer by controlling the level of electrolysis voltage in the ionizer. In general, 1stage (pH8), 2stage (pH8.5), 3stage (pH9), 4stage (pH9.5) are used as the alkaline ionized water, -1Stage (pH6.0), -2 stage (pH5.0) are used as the acidic water. But in early stage, the water that passed through filter was weakly alkaline water and that was problem. Therefore, when filter condition is stable, the pH and ORP value of water is different with the early one. the initial setting pH value of the ionizer was confirmed that changes significantly. In order to resolve this problem we need to wash filter for some period time and neutralize by acidification treatment of the filter.

• Journal of dental hygiene science
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• v.12 no.4
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• pp.303-309
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• 2012

This study was designed to provide basic data for developing a standardized caries potentiality index to help to choose snack foods with a low score on the index by investigating adolescents' snack intakes and measuring them in total saccharinity, pH, and acidogenic potential and glucosidase activity of Streptococcus mutans (S. mutans). Total 28 snack foods were selected and measured for total saccharinity (Pocket refractometer PAL-1, ATAGO) and pH with a pH meter (Mentor, Seoul, Korea). Artificial saliva was added to each sample. The experiment group was administered with S. mutans (ATCC 3692), cultured in a constant temperature incubator at $37^{\circ}C$, and measured for pH changes over five times including after 10 minutes, 30 minutes, 1 hour, and 24 hours. Each sample of 0.3 ml was added to tubes containing sucrose, galactose, or glucose to measure the glucosidase activity of S. mutans. They were then observed for glucosidase activity with colorimetry after 24 hours of culture in a constant temperature incubator at $37^{\circ}C$. The mean pH by the acidogenic potential of S. mutans was pH 5.33. The experiment group dropped in pH more than the control group due to the increasing acidogenic potential of S. mutans by glucosidase activity, recording pH 5.27 after 10 minutes, pH 5.21 after 30 minutes, pH 5.15 after 1 hour, and pH 4.80 after 24 hours. The observation results of glucosidase activity of S. mutans with colorimetry show that most of the samples were positive in orange and yellow with glucose, sucrose, and glactose recording activity of 78.58%, 75%, and 71.42%, respectively.

• Journal of Korean Society of Environmental Engineers
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• v.29 no.1
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• pp.54-61
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• 2007

The influences of pH were investigated for anaerobic hydrogen gas production under the constant pH condition ranged from pH 3 to 10. Carbon dioxide and hydrogen gas were main components of the gas but methane was not detected in the produced gas when sucrose was added in enrichment medium. When the modified Gompartz equation was applied for the statistical analysis of experimental data, a hydrogen production potential and maximum gas production rate at pH 5 were 1,182 mL and 112.46 mL/g dry wt biomass/hr. The hydrogen conversion ratio was 22.56%. The butyrate/acetate ratios at pH 5 and pH 6 are 1.63 and 0.38. Higher butyrate/acetate ratio produced more hydrogen gas generation. The Haldane equation model was used to find the optimum pH and fitted well with the experimental data$(r^2=0.98)$. The optimum pH and specific hydrogen production were 5.5 and 119.61 mL/g VSS/h.

• Parasites, Hosts and Diseases
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• v.27 no.3
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• pp.161-170
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• 1989

The proteases of Toxoplasma gcndii were purified partially and characterisrd for some biochemical properties including various chromatographic patterns, major catalytic classes, and conditions to promote the activity of these enzymes. When Toxoplasma extract was incubated with 3H-casein at various pH, peak hydrolysis of casein was observed at pH 6.0 and at pH 8.5. Proteasfs working at pH 6.0 and at pH 8.5 were purified partially by conventional methods of chromatographies of DE52 anion rxchange, Sephadex G-200 gel permeation, and hydroxylapatite chromatography. Partially purified enzymes were tested by site-specific inhibitors and promotorf. The protease working at pH 6.0 was inactivated by iodoacetamide with LDso of 10-5 M and promoted by dithiothreitol, while the protease working at pH 8.5 was inhibited by phenylmethylsulfonyl fluoride with LD50 of 10-5 M and was Promoted by ATP (excess ATP beyond 2 mM inhibited the activity reversely). The protease of pH 8.5 had the activity of ATPase which might exert the energy to its action. Therefore the former was referred to as a cysteinyl acid protease and the latter, ATP-dependent neutral serine protease.

• KSBB Journal
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• v.10 no.5
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• pp.568-574
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• 1995

To investigate the effect of pH on organic acid production by Anaerobiospirillum succiniciproducens, an anaerobic fermentation was carried out by maintaining the pH of the fermentation broth at 5.8, 6.0, 6.4, 6.8, and 7.2. At various pHs, the concentrations of cell were $1.0∼1.9g/\ell$ which were two to three times higher than those of the other worker's results, and the maximum was obtained at pH 5.8. Substrate consumption was increased by increasing the pH in the range of pH 6.0 to 6.8, while the sugar consumption rate at both pH 5.8 and 7.2 was very slow. The total amount of 2M $Na_2C0_3$ added for adjustment of pH change due to organic acid production was maximum at pH 6.8. Changes of conductivity of the fermentation broth was very simillar to those of 2M $Na_2C0_3$ added at various pHs. Therefore, it is suggested that determination of the amount of organic acid in a broth can be possible by measuring the conductivity. The maximum production yield of lactate based on glucose was 64% for pH 7.2 and 32% for pH 6.8, respectively.

• Food Science of Animal Resources
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• v.35 no.6
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• pp.841-846
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• 2015

This study was investigated to determine the effect of microbial transglutaminase (MTG) with or without red bean protein isolate (RBPI) on the porcine myofibrillar protein (MP) gel functionality at different pH values (pH 5.75-6.5). Cooking yield (CY, %), gel strength (GS, gf), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM) were determined to measure gel characteristics. Since no differences were observed the interaction between 1% RBPI and pH, data were pooled. CY increased with the addition of 1% RBPI, while it was not affected by pH values. GS increased with increased pH and increased when 1% RBPI was added, regardless of pH. There were distinctive endothermic protein peaks, at 56.55 and 75.02℃ at pH 5.75, and 56.47 and 72.43℃ at pH 6.5 in DSC results, which revealed decreased temperature of the first peak with the addition of 1% RBPI and increased pH. In SEM, a more compact structure with fewer voids was shown with the addition of 1% RBPI and increased pH from 5.75 to 6.5. In addition, the three-dimensional structure was highly dense and hard at pH 6.5 when RBPI was added. These results indicated that the addition of 1% RBPI at pH 6.5 in MTG-mediated MP represent the optimum condition to attain maximum gel-formation and protein gel functionality.

• Journal of the Korean Chemical Society
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• v.28 no.5
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• pp.328-334
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• 1984

A series of phenyl N-benzenesulfonylchloroformimidate derivatives (p-H, p-Cl, p-CH3 & p-OCH3) were prepared and the hydrolysis of these compounds were studied kinetically at various pH by UV spectrophotometry in 1 ; 4 dioxane-water at $25^{\circ}C$. Hammett ${\rho}$ values measured at pH 5.0 (${\rho}$ = -0.45) and pH 10.0 (${\rho}$ = 0.40) indicate that the reaction proceeds via an azocarbonium ion intermediate in the acidic medium, whereas, it involves direct attack by hydroxide ion on the azomethine carbon atom occurs under the basic medium. The formation of stabilized azocarbonium ion species at pH 5.0 is also consistent with the large solvent effect(m = 1.3-1.5 & n = 5.0-5.5). On the basis of these findings, we may concluded that the hydrolysis of phenyl N-benzenesulfonylchloroformimidate derivatives proceeds by $SN_1$ below pH 8.0, however, above pH 10.0, the hydrolysis proceeds through $SN_2$ and in the range of pH 8.0-10.0, these two reactions occur competitively.

• Korean Journal of Food Science and Technology
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• v.22 no.2
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• pp.177-182
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• 1990

The changes in the partition coefficient of model proteins (lysozyme, myoglobin, conalbumin, bovine serum albumin) in an aqueous two·phase system formed by polyethylene glycol and dextran were examined in order to improve the capacity of counter current distribution (CCD) for the protein fractionation and concentration . The protein distribution pattern in CCD with 30 tubes varied with the pH (4.5, 5.5, 6.5, 9.0, 12.0) and KCl concentration (0mM, 50mM, 250mM, 500mM) of the system. From the mixture of model proteins, pure myoglobin was appeared at the upperphase of 14th tube having 50mM of KCl at pH 5.5 and the upper-phase of 13th tube having 250mM of KCl at pH 6.5. Similarly pure BSA was obtained at the 14th tube having KCl 250mM with pH 4.5, pure lysozyme at the 19th tube having 500mM of KCl at pH 4.5 and the upper-phase of 16th tube 50mM of KCl at pH 5.5.

• Journal of Animal Science and Technology
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• v.47 no.5
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• pp.851-856
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• 2005

The aim of this experiment was to evaluate the stability of anti-Helicobacter pylori IgY in water soluble fraction(WSF) of egg yolk according to the heat, pH and digestive enzyme treatment. Anti-H. pylori IgY content of WSF remained 76% after pasteurization(63$^{\circ}C$ for 30 min). The stability of anti-H. pylori IgY at different pH showed a tendency to diminish according to decreasing pH from 7.0 to 1.5(p＜0.05). Anti-H. pylori IgY content was 84.4% after treatment for 1 hour at 37$^{\circ}C$ in pH 5.0. There were significantly differences in IgY content between 1 hour and 2 hours at pH 2.0 in 200 units of pepsin treatment(p＜0.05). However, IgY was relatively stable at pH 4.0 regardless of the reaction time and the concentration of pepsin. The stability of IgY of egg yolk after the treatment of trypsin was significantly higher than that of water soluble fraction (p＜0.05). This results indicated that anti-H. pylori IgY showed relatively a good stability on heat, pH and digestive enzyme.