• The Journal of the Korean dental association
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• v.57 no.5
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• pp.264-268
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• 2019

Objectives: This study aimed to measure the water sorption / solubility of Biodentine, composite resin and glass ionomer cement. Materials and Methods: The materials used in this study were Biodentine(BD), Filtek Z250(FZ) and Ketac Molar(KM). Twenty disc-shaped specimens of each material were prepared of 6mm diameter and 1mm thickness. All specimens were desiccated for 24 hours and weighed(m1). After then, They were immersed in distilled water and stored at $37^{\circ}C$. 1 week later, They were washed with running water, wiped with absorbent paper and weighed(m2). Finally, They were dried for 24 hours and weighed(m3). Water sorption and solubility, net water uptake were calculated. Results: KM and BD showed high water sorption than FZ(P<0.05). KM and BD exhibited similar water sorption(P<0.05). BD exhibited high solubility than KM(P=0.012). BD exhibited high net water uptake than FZ(P=0.008). Conclusion: Biodentine showed higher water sorption, solubility and net water uptake than Filtek Z250 and Ketac Molar. Within limitation of this study, it is not recommended to use Biodentine for permanent restoration.

• Applied Biological Chemistry
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• v.32 no.4
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• pp.321-326
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• 1989

Nitrogen and phytate solubility of perilla seed flour were influenced by the following factors: pH, centrifugal force, temperature and the presence of salt. The nitrogen solubility of perilla seed flour was minimum$(17.1{\sim}18.0%)$ at the pH range of $(4.0{\sim}5.0)$ and maximum(92.3%) at pH 11.0, while phytate solubility was the highest(48.5%) at pH 4.8 and lowest(8.3%) at pH 11.0. The phytic acid content in the extract decreased with an increase in centrifugal force. However, the nitrogen content was not affected by centrifugal force. The solubility of nitrogen and phytate gradually increased as the temperature was increased from $5^{\circ}C$ to $60^{\circ}C$ The addition of calcium$(0{\sim}50mM)$ at pH 5.0 decreased the phytate solubility, but increased nitrogen solubility. The solubility of nitrogen and phytate of perilla seed protein isolate was gradually increased as pH raised further. The protein and phytate contents of the perilla seed protein isolate were 1.1 and 89.6%, respectively, compared to 5.0 and 60.1% for perilla seed flour.

• Journal of the Korean Applied Science and Technology
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• v.25 no.4
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• pp.429-437
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• 2008

The p-dioxanone can be used to make a variety of commercially useful products particularly where biodegradability is desired, such as fibers, sutures, molded articles, containers, medical devices and surgical clips, film and compostable trash bags. The mole fraction solubility of p-dioxanone in various solvents such as acetone, ethylacetate, tetrahydrofuran, methanol, ethanol, 1-propanol, 1-butanol and 1-pentanol were measured over the temperature range from 263.05 K to 288.45 K. The solubility of p-dioxanone increases with increasing polarity of the solvents.

• Korean journal of food and cookery science
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• v.6 no.3 s.12
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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.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.8
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• pp.1159-1165
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• 2016

The nutritional value of feed proteins and their utilization by livestock are related not only to the chemical composition but also to the structure of feed proteins, but few studies thus far have investigated the relationship between the structure of feed proteins and their solubility as well as digestibility in monogastric animals. To address this question we analyzed soybean meal, fish meal, corn distiller's dried grains with solubles, corn gluten meal, and feather meal by Fourier transform infrared (FTIR) spectroscopy to determine the protein molecular spectral band characteristics for amides I and II as well as ${\alpha}$-helices and ${\beta}$-sheets and their ratios. Protein solubility and in vitro digestibility were measured with the Kjeldahl method using 0.2% KOH solution and the pepsin-pancreatin two-step enzymatic method, respectively. We found that all measured spectral band intensities (height and area) of feed proteins were correlated with their the in vitro digestibility and solubility ($p{\leq}0.003$); moreover, the relatively quantitative amounts of ${\alpha}$-helices, random coils, and ${\alpha}$-helix to ${\beta}$-sheet ratio in protein secondary structures were positively correlated with protein in vitro digestibility and solubility ($p{\leq}0.004$). On the other hand, the percentage of ${\beta}$-sheet structures was negatively correlated with protein in vitro digestibility (p<0.001) and solubility (p = 0.002). These results demonstrate that the molecular structure characteristics of feed proteins are closely related to their in vitro digestibility at 28 h and solubility. Furthermore, the ${\alpha}$-helix-to-${\beta}$-sheet ratio can be used to predict the nutritional value of feed proteins.

• YAKHAK HOEJI
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• v.37 no.3
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• pp.216-227
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• 1993

Complex formations of practically insoluble antelmintic drugs such as mebendazole (MBZ), albendazole (ABZ) and flubendazole (FBZ) with dimethyl-$\beta$-cyclodextrin (DM-$\beta$-CyD) and 2-hydroxypropyl-$\beta$-cyclodextrin (HP-$\beta$-CyD) together with $\alpha$-, $\beta$- and $\gamma$-cyclodextrins(CyDs) in duffered solutions were investigated by solubility method. $A_{L}$ type phase solubility diagrams were obtained in all cases except for the complexation (B$_{s}$, type) of FBZ with $\gamma$-CyD. The highest stability constants were obtained with DM-$\beta$-CyD, followed by $\alpha$-CyD > $\beta$-CyD > HP-$\beta$-CyD > $\gamma$-CyD for ABZ, and HP-$\beta$-CyD > $\gamma$-CyD > $\beta$-CyD > $\alpha$-CyD for FBZ at pH 1.2. On the other hand, solid dispersion systems of ABZ and FBZ with $\beta$- and DM-$\beta$-CyDs were prepared by solvent evaporation method and evaluated by dissolution, differential thermal analysis and powder x-ray diffractometry. The dissolution rates of ABZ- and FBZ-DM-$\beta$-CyD solid dispersions were much faster than those of drugs alone, corresponding physical mixtures and tablets on market both at pH 1.2 and 6.8. Although dissolution rates of all samples at pH 6.8 were by far lower than those obtained at pH 1.2, as explained by pH-solubility profiles for ABZ and FBZ, the dissolution rates at pH 6.8 of ABZ from $\beta$- and DM-$\beta$-CyD solid dispersions exceeded the respective equilibrium solubility (23.9 $\mu\textrm{g}$/ml). Fast dissolution of ABZ from solid dispersions with CyDs was attributed to the reduction of drug crystallinity and particle size which was supported by DTA and powder x-ray diffractometry. Consequently these results suggest that solid dispersion systems with CyDs may provide useful means to markedly enhance the solubility and dissolution of benzimidazole antelmintic drugs.

• Korean journal of food and cookery science
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• v.9 no.1
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• pp.43-51
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• 1993

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 $80^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.279-283
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• 1992

This study was undertaken to investigate the effects of added phytate and pH on the solubility and in vitro digestibility of low-phytate rapeseed protein isolate. Phytate content of low-phytate rapeseed protein isolate was 1.5%, as a result of 66% removal from defatted rapeseed flour and the protein: phytate ratio was 58:1. Solubility of rapeseed protein isolate at pH 2.0 and pH 11.5 was much higher than near the isoelectric point, pH 5.0. It's solubility was lowered by adding an increased amount of phytate especially at pH 2.0. The inhibitory effect of phytate toward pepsin digestibility of rapeseed protein isolate decreased by the increasing amount of phytate added. It is suggested that the production of low-phytate rapeseed protein isolate is necessary to improve the functionality and nutritional value in order to utilize it as food material.

• Journal of Pharmaceutical Investigation
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• v.29 no.3
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• pp.205-210
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• 1999

To formulate the parenteral delivery of a new cephalosporin derivative, 7-${\beta}$-[(2)-2-(2-arninothiazol-4-yl)-2methoxyiminoacetamido]- 3- [(2,3-cyclopenteno-4-carbamoyl-l-pyridinium)methyl]- 3-cephem-4-carboxylate sulfate( CKD604), the stability and solubility of CKD-604 in various aqueous media were investigated. The degradation kinetics of CKD-604 in aqueous solutions (ionic strength 0.1, pH 1-8) were studied at $37^{\circ}C$. The observed degradation rates followed pseudo first order kinetics. The pH-rate profile exhibited a minimum degradation rate at pH 5. The Arrhenius activation energy was 14.2 kcal/mol in pH 5 buffer solution. Excellent agreement between the cephalosporins' theoretical pH-rate profile and the experimental data indicated that the degradation pathway of CKD-604 could be predicted according to the general pathway of cephalosporins. The solubility of CKD-604 was 8.16 mg/ml at $25^{\circ}C$. To enhance the solubility and adjust the suitable pH, CKD-604 was solubilized by using sodium ascorbate, ascorbic acid and urea. The compositions were obtained to satisfy optimum pH and concentration, and the total amount of additives was several times of the active ingredient, CKD-604.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.67-70
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• 1998

In order to understand the influence of ferroxidase center on the protein assembly and solubility of tadpole ferrin, three mutant plasmids, pTH58K, pTH61G, and pTHKG were constructed with the aid of site-directed mutagenesis and mutant proteins were produced in Eshcerichia coli. Mutant ferritin H-subunits produced by the cells carrying plasmids pTH58K and pTHKG were active soluble proteins, whereas the mutant obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence of sorbitol and betaine. Especially, the cells carrying pTH61G together with the plasmid pGroESL harboring the molecular chaperone genes produced soluble ferritin. The mutant ferritin H-subunits were all assembled into ferritin-like holoproteins. These mutant ferritns were capable of forming stable iron cores, which means the mutants are able to accumulate iron with such modified ferroxidase sites. Further functional analysis was also made on the individual amino acid residues of ferroxidase center.