The purpose of this study was to determine the foaming properties of two small red bean protein isolates at various conditions. Data concerning the effects of pH, temperature, MaCl concentration, sugar concentration and protein concentration on the properties such as solubility, foam expansion, foam stability were presented. The results were summarized as follows : 1. The crude protein contents of two small red beans were 26.14% and 22.71%. The percentage of nonpolar amino acid group was the highest and that of sulfur containing amino acid group was the lowest. 2. Protein solubility showed the minimum at pH 4.5 which is isoelectric point of small red bean protein isolate adn heat treatment lowered solubility(P<0.05). At pH 4.5, solubility increased sighificantly as 0.4M NaCl was added. However, the effect of sugar concentration in the solubility was not significant. 3. Foam expansion of two small red bean protein isolates was high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam expansion(P<0.05). While addition of NaCl, sugar did not affect the foma expansion, gradual increment of the protein isolates concentration up to 9% decreased the foma expansion slightly. 4. Foam stability was significantly high at pH 4.5 and heat treatment at 10$0^{\circ}C$ lowered foam stability. Addition of sugar caused slight decrease in foam stability. From 1% to 9% suspension, foma stability increased significantly as protein concentration increased(P<0.05)
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.
1. The sericin solubility increased rapidly as the increase of water M-alkalinity. 2. The acidity of the treated water was nutralized at the over 25ppm of M-alkalinity. 3. The more M-alkalinity of the sample water is, the more M-alkalinity was found after cocoon treat. 4. The total hardness of sample water seemed to be droped as M-alkalinity increased. 5. The sericin solubility also seemed to be droped as the increase of water acidity. 6. In case of treat finish with cocoon, the acidity and total hardness seemed to increase as the acidity of the water increased, but M-alkalinity was nutralized at 20~40 ppm of water acidity or the M-alkalinity could not be found in case over 40ppm of acidity. 7. In case increase of iron component with sample water, sericin solubility seemed to drop down, and mangan component showed the same nature but dull drop. 8. After cocoon was treated with water, acidity, M-alkalinity and total hardness were increased by the extraction from cocoon shell because of pH and treating temperature but not because of iron componnent. Mangan component, however, affected as to increase of acidity and total hardness but to decrease for M-alkalinity. 9. In case change of M-alkalinity and total hardness, sericin solubility has increased also. 10. In case constant pH and total hardness, the more M-alkalinity is, the more sericin solubility was found. 11. In case constant pH, total hardness, and M-alkalinity, the more acidity is, the less sericin solubility was found. 12. In case constant pH(6.8) and M-alkalinity, the more total hardness is, the less sericin solubility was found. 13. Though the combination of water, high solubility water, medium solubility water and low solubility water were prepared. The high solubility water desolved sericin 2.2% more than low solubility water. And the medium solubility water desolved sericin as much as 2.4~2.9%. 14. It was found that the most important factors for filature water are pH, M-alkalinity, acidity and total hardness which may need more words for optimum filature water development. 15. In case of repeat use of water, the buffer action of water has increased so that the sericin solubility to be decreased.
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.
Physicochemical properties of aspalatone (acetylsalicylic acid maltol ester, AM), which has been recently found to have an antithrombotic effect, were studied in terms of solubility, dissolution, partition coefficient (Pc) and stability. The solubility of AM at 37$^{\circ}C$ was about 1.2 mg/ml and the P$_{c}$ value for n-octanol/water and chloroform/water was 11.4 and 382.6, respectively. Dissolution rates of AM at pH 1.2 and 6.8 were more than 80% within 30 min. The degradation of AM followed apparent first-order kinetics, and was dependent on temperature, pH and ionic strength. From the pH-rate profile, the optimal pH was found to be at around 4.0. Half-lives at pH 1.2 and 6.8 were 33.5 and 44.4 hr, respectively. The degradation rate of AM at pH 1.2 was somewhat faster than that of aspirin, but at pH 7.0, the degradation rate of AM was slower than that of aspirin.n.
Park, Yong-Joon;Pyo, Hyung-Ryul;Kim, Won-Ho;Chun, Kwan-Sik
Journal of the Korean Chemical Society
/
v.40
no.9
/
pp.599-606
/
1996
The effects of chemical species in groundwater on the solubility of the uranyl hydrolysis precipitates formed at pH 6.4 and 9.7 were investigated. Based on the chemical composition of the groundwater, the synthetic groundwater was prepared. The colloid-free (separated) groundwater was also prepared by removal of both organic and inorganic colloids from the sampled groundwater. Solubilities of precipitates formed in the hydrolysis of uranyl ion in groundwater, separated groundwater, synthetic groundwater and 0.1 M NaCl solution were measured over neutral to alkaline pH range, and especially, the effect of the anions and cations found in groundwater on the solubility was investigated. Solubility in groundwater was approximately two orders of magnitude greater than that in 0.1 M NaCl solution. Soubililties of uranyl hydrolysis precipitates formed at pH 9.7 and 6.4 were compared in groundwater and synthetic groundwater. Solubilities of the precipitates formed at different pH were found to be in the same order of magnitude in groundwater and synthetic groundwater, however the uranyl hydolysis precipitates formed at higher pH values showed a tendency of higher solubility.
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.
In this paper, the effects of crosslinking agent and pH controlling agent on adhesive properties and water solubility of water soluble acrylic pressure sensitive adhesives were studied by adding the crosslinking agents or pH controlling agents after the polymerization. the tack, cohesive strength, and peel strength were measured to evaluate adhesive properties. the turbidity was also measured to evaluate water solubility of pressure sensitive adhesives. When crosslinking agent was added less than 0.2 wt%, tack increased and cohesive strength and peel strength decreased with increasing concentration. When crossinking agent was added more than 0.2 wt%, the results were opposited. When pH controlling agent was added, tack and water solubility decreased and peel strength and cohesive strength increased with increasing concentration. the influence of pH controlling agents on adhesive properties and water solubility of pressure sensitive adhesive increased in the order of lithium hydroxide, potassium hydroxide and sodium hydroxide.
Sohn, Kyung-Hee;Min, Sung-Hee;Park, Hyun-Kyung;Park, Jin
Korean journal of food and cookery science
/
v.7
no.2
/
pp.97-104
/
1991
This study was carried out in order to study the protein functionality such as foaming and emulsifying properties by succinylation of peanut protein isolates. Succinylated and unsuccinylated peanut protein isolate was tested for to find out the effect of pH, heat treatment and sodium chloride concentration on the solubility, foam expansion, foam stability, emulsion capacity and emulsion stability. The results are summarized as follows; 1. Succinylation enhanced the solubility of peanut protein isotate (PPI). The solubility of succinylated PPI markedly increased at pH 4.5. When the protein solutions was heated, the solubility of succinylated PPI greatly increased than PPI at pH 3. With addition of NaCl, solubility of succinylated PPI increased at pH 7 and pH 9. 2. The foam expansion of PPI and succinylated PPI on pH was no difference between both proteins. Addition of NaCl and heat treatment caused steeply increased in foam expansion at pH 3. 3. The foam stability of PPI and succinylated PPI showed the lowest value at pH 4.5. When PPI and succinylated PPI was heated, foam stability of two proteins incensed at pH 3 and showed similar aspects between PPI and succinylated PPI. However, at pH 9 stability of succinylated PPI decreased by heat treatment over $60^{\circ}C$. 4. Emulsion capacity of succinylated PPI on pH was markedly increased and showed the highest value at pH 11. At pH 4.5 which is isoelectric point of PPI, emulsion capacity of PPI by succinylation improved than that of PPI. When succinylated PPI was heated, emulsion capacity was greatly increased at pH 2 and pH 7. With NaCl was added, emulsion capacity of succinylated PPI increased than that of PPI. 5. Emulsion stability of PPI and succinylated PPI was affected by pH and showed its highest value at pH 11. At pH 4.5, emulsion stability of succinylated PPI increased than that of PPI. Addition of NaCl and heat treatment caused slightly increased in emulsion stability of succinylated PPI.
This experiment was carried out to study changes in solubility and emulsifying properties of whey protein. Whey protein hydrolysates were obtained from tryptic hydrolysis of whey protein concentrate at pH 8.0 and 37$^{\circ}C$ for 6 hours. Emulsifying activity of whey protein hydrolysate was highest at 4 hours of hydroysis and at 5.50% of DH. During hydrolysis of whey protein concentrate with trypsin, ${\alpha}$-lactalbumin was not easily broken down. But ${\beta}$-lactoglobulin was hydrolysed rapidly from the early stage of hydrolysis, producing several low molecular weight peptides, which have to participate in increasing emusifying activity. The solulbility of hydyolysates tended to increase depending on hydrolysis time; however, there was a gradual decrease after 5 hours. The hydrolysate had a minimum solubility near the isoelectric point range (pH 4∼5). The more hydrolysed the whey protein concentrates, the more soluble they are near the pl. They aye also more soluble above pH 6. Emulsifying activity of hydrolysates showed similar results to solubility. Creaming stability gradually increased when hydrolysis increased, increasing rapidly above pH 8 after 4 hours of hydrolysis.
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