• Archives of Pharmacal Research
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• 제24권2호
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• pp.159-163
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• 2001

The accelerated stability of dimethoxy biphenyl monocarboxylate.HCl (DDB-S) was investigated in 6 mg/mL water solution in the pH ranging 2-10 and the temperature of $45-85^{\circ}C$. The observed rate of degradation followed first-order kinetics. The energy of activation for DDB-S degradation was calculated to be 14.1 and 16.5 $Kcal/mole$ at pH 5 and in distilled watery respectively. The degradation rate constant ($K_{25^{\circ}C}$) obtained by trending line analysis of Arrhenius plots for DDB-S was $5.3{\times}10^{-6}h^{-1}$. The times to degrade 10% ($t_{10}$) and 50% $t_{500}$) at $K_{25^{\circ}C}$ were 829 and 5,416 days, respectively. DDB-S exhibited the fastest degradation at pH 10 and the slowest rate at pH 5. In addition, at $K_{65^{\circ}C}$, degradation rate constants of DDB-S were 0.066, 0.059, 5.460, 32.171, and $1.4{\times}10^{-6}h^{-1}$ at pH 2, 5, 8, 10 and in distilled water, respectively. These observations indicated that the rate-pH profile of DDB-S showed general acid-base catalysis reaction in the range of pH 2-10.

• Archives of Pharmacal Research
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• 제20권6호
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• pp.643-646
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• 1997

Thermal stability of a red pigment, carthamin, frm Carthamus tinctorius was investigated to explore possible applications as natural color additives for foods, cosmetics, and nutraceuticals. Degree of degradation reactions of carthamin at acidic, neutral and alkaline conditions were determined with UV/V is spectral measurements. Decomposition half lives of carthamin at 25.deg. C were 4.0 h, 5.1 h, and 12.5 h at pH 5.0, pH 7.0, and pH 12.0, respectively, indicating that carthamin is much more stable at alkaline pH than acidic or neutral conditions. The activation energies of carthamin at pH 5.0, pH 7.0, and pH 12.0 were 15.6, 15.7 and 16.8 kcal/mol, respectively.

• 약학회지
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• 제20권1호
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• pp.27-31
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• 1976

The stability of a newly introduced anthelmintic, mebendazole, in sweetened and aqueous suspension was tested by the accelerated temperature method and the effect of pH on the stability of mebendazole was studied. Mebendazole in aqueous and sweetened suspension was very stable at the pH range from 4 to 8.

• 한국식품과학회지
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• 제31권1호
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• pp.106-109
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• 1999

S. epidermidis에 의해 치자황색소에서 변환된 청녹계색소와 치자황색소의 저장안정성에 미치는 광, 온도, pH, 무기이온에 의한 영향을 조사하였다. 두 색소는 광과 $40^{\circ}C$ 이상의 온도조건에서 변색에 영향을 받았으나, 변환된 색소가 보다 안정성이 있으며, 광에 의한 영향은 green filter에 의해 감소시킬 수 있었다. pH와 무기이온에 의한 영향은 두 색소 모두 작았다.

• Journal of Pharmaceutical Investigation
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• 제41권4호
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• pp.233-238
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• 2011

DEET, N,N'-diethyl-m-toluamide, is the most commonly used mosquito repellent. However, it can easily permeate through skin leading to toxic effects. A recent study showed that the ortho analogue of DEET showed enhanced repellency with reduced permeation compared to the commercially used meta analogue. Thus, in order to understand the differences in properties and effectiveness among the m-, o- and p-analogues of DEET, an HPLC-UV method was developed for separately analyzing the three analogues. Moreover, stability profiles at temperatures ranging from $30^{\circ}C$ to $70^{\circ}C$ as well as pH ranging from pH 3 to pH 9 have been determined. All three analogues were stable with no degradation observed during the 5 day period. o-DEET therefore could be further developed into a safer and more effective mosquito repellent.

• Biomolecules & Therapeutics
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• 제1권1호
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• pp.31-36
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• 1993

To evaluate the feasibility of transmucosal delivery of methionine enkephalin analog, [$D-Ala^2$]-me-thionine enkephalinamide (YAGFM), the influence of pH, temperature, ionic strength and initial peptide concentration on the physicochemical stability of YAGFM in aqueous buffered solutions were investigated using a stability-indicating HPLC method. The degradation of YAGFM followed the pseudo-first-order kinetics. From the pH-rate profile, the maximum stability of YAGFM was shown to be at the pH of about 5.0. The halflife for the degradation of YAGFM was found to be 181.3 days at pH 5.0 and $37^{\circ}C.$ Arrhenius plots of the data obtained at 25~$45^{\circ}C$ were reasonably linear with a correlation coefficient greater than 0.99, and the activation energy was calculated to be 8.9 kcal/mole. A higher ionic strength and/or a higher peptide concentration in buffered solutions retarded the degradation of YAGFM.

• Bulletin of the Korean Chemical Society
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• 제34권9호
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• pp.2663-2670
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• 2013

The purpose of stability testing is to provide evidence about how the quality of a drug varies with time under the influence of a variety of environmental factors. In this study, erythropoietin (EPO) was analyzed under different pH (pH 3 and pH 9) and temperature ($25^{\circ}C$ and $40^{\circ}C$) conditions according to current Good Manufacturing Practice (cGMP) and International Conference on Harmonisation (ICH) guidelines. The molecular weight difference between intact EPO and deglycosylated EPO was determined by SDS-PAGE, and aggregated forms of EPO under thermal stress and high-pH conditions were investigated by size exclusion chromatography. High pH and high temperature induced increases in dimer and high molecular weight aggregate forms of EPO. UPLC-ESI-TOF-MS was applied to analyze the changed modification sites on EPO. Further, normal-phase high-performance liquid chromatography was performed to identify proposed glycan structures and high pH anion exchange chromatography was carried out to investigate any change in carbohydrate composition. The results demonstrated that there were no changes in modification sites or the glycan structure under severe conditions; however, the number of dimers and aggregates increased at $40^{\circ}C$ and pH 9, respectively.

• 미생물학회지
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• 제13권2호
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• pp.59-63
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• 1975

When the enzyme preparations were at various temperatures for 1 hour, the thermal stability for the enzyme was maximum at $30{\circ}C.$ The optimum temperature for the enzyme activity was at $40{\circ}C.$ When the enzyme preparations were exposed to various pHs for 22 hours, the enzyme stability was maximum at pH 3.8, and it was decreased gradually as the pH rose up to 4.8, above which the stability was greatly restored. When the exposure period was extended from 22 to pH's 3.0 and 5.9, but the stability tended to rise at pH's below 3.0 and above 5.9. The optimum pH for the enzyme activity was obtained at 4.8.

• 한국식품조리과학회지
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• 제6권3호통권12호
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• pp.9-15
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• 1990

Peanut prptein isolate was tested for the purpose of finding out the effect of pH, Sodium Chloride concentration and heat treatment on the solubility, surface hydrophobicity, foam expansion and foam stability. The solubility of peanut protein isolate was affected by pH and showed the lowest value at pH 4.5. When the peanut protein isolate was heated, the solubility decreased at pH 3 and pH 7 but at pH 9 solubility increased. At all pH range, solubility decreased as NaCl was added. The surface hydrophobicity of peanut protein isolate showed the highest value at pH 1.5. Generally, at acidic pH range the surface hydrophobicity was high, but at alkaline region, the surface hydrophobicity increased as the temperature increased. And when NaCl was added, the surface hydrophobicity was also increased. Foam expansion of peanut protein isolate was no significant difference among the values about pH. When the peanut protein was heated and NaCl was added, foam expansion was increased at pH 7. Foam stability was significantly low at pH 4.5 and foam stability was increased at acidic pH region below pH 4.5. At pH 7 and pH 9, heat treatment above $60^{\circ}C$ increased foam stability. When NaCl was added, foam stability was significantly increased at pH 3 and pH 7.

• 한국식품조리과학회지
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• 제6권4호통권13호
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• pp.9-14
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• 1990

The emlsifying properties of small red bean protein isoates were evaluated through their emulsion capacity and stability of the resulting emulsions. The influence of pH, Sodium Chloride and heat treatment on the efficiency of small red bean protein isolates as emulsifying agents was studied. The surface hydrophobicity (So) of small red bean protein islates also examined. The results were obtained as follows; 1. The emusion capacity of small red bean protein isolates was high at pH 11, low at pH 3 and decreased by heat treament. With addition of NaCl, emulsion capacity decreased steadily and showed lowest value when 0.2M NaCl was added. 2. The emulsion stability at pH 4.5 and heat treatment over $60^{\circ}C$ decreased emulsion stability at pH 4.5. When NaCl was added, emulsion stability was generally increased. 3. The surface hydrophobicity of small red bean protein isolates showed the highest value at pH 3 and lowest at pH 11 and increased as the heating temperature increased When 0.2 M NaCl was added, surface hydrophobicity also increased at pH 4.5.