• The Korean Journal of Food And Nutrition
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• v.13 no.4
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• pp.348-352
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• 2000

The stabilization of wheat $\beta$-amylase( Himaltosin GL, Hankyu-Bio) was attained by modification wish periodate-oxidized soluble starch. The specific activities of modified enzyme at pH 9.7 and pH 8.0 were 17% and 96%, respectively, compared with that of native enzyme. The pH stability of modified enzyme was increased at pH 2~5 and 6~12 in the presence of $\alpha$-cyclodextrin( $\alpha$-CD) compared with that of native enzyme, and optimum pH of the enzyme was changed from pH 5.0 to pH 7.0 by the modification. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 10min, the activity remained 8% for the enzyme modified at pH 8.0 in the presence of $\alpha$-CD and tested in the presence of $\alpha$-CD, 5% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The molecular weight of the modified enzyme was slightly increased in HPLC analysis.

• Bulletin of the Korean Chemical Society
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• v.32 no.2
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• pp.498-502
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• 2011

The divergent synthesis of novel phosphorus-containing dendrimer with 4,4'-sulphonyldiphenol at the core has been accomplished involving simple condensation reactions using $P(O)Cl_3$, $P(S)Cl_3$, 3-amino-phenol, 3-hydroxy-benzaldehyde, and 2-butyn 1, 4-diol. The final compound was a Schiff's base macromolecule possessing 4 imine bonds, 8 acetylenic bonds and 8 OH groups at the periphery. The structures of intermediate compounds were confirmed by IR, NMR ($^1H$, $^{13}C$ and $^{31}P$), LC-Mass and C, H, N analysis. The structure of the final dendrimer (5) was confirmed by IR, NMR ($^1H$, $^{13}C$ and $^{31}P$), MALDI-TOF-MS, and C, H, N analysis. The surface morphological characteristics of the final dendrimer were understood by Scanning Electronic Microscopic study (SEM). The thermal stability of the final dendrimer was studied by TGA/DTA analysis.

• The Korean Journal of Food And Nutrition
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• v.12 no.3
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• pp.265-270
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• 1999

The stabilization of Aspergillus sp. $\alpha$-amylase was attained by modification with periodate-oxidized sol-uble starch. The pH stability of modified enzyme was increased at pH 3~4 and 9~11 in the presence of $\alpha$-cyclodextrin($\alpha$-CD) compared with that of native enzyme. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 30min the activity remained 20% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD and tested in the presence of $\alpha$-CD 10% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD 0% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The substrate specificity of the modified enzyme was not changed in HPLC analysis of reaction product.

• Journal of the Korean Ceramic Society
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• v.36 no.7
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• pp.705-710
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• 1999

Stability and chemical durability for aqueous casting of BaTiO3 slurry with polycarylic acid(PAA) were studied. PAA was well chemisorbed on surface of BaTiO3 powder at neutral pH but did not chemically adsorbed at low pH. The amount of Ba dissolution in aqueous BaTiO3 slurry was abruptly increased at strong acid pH2 and also at high amount of PAA. Protection of Ba dissolution and stability of slurry could be obtained through the optimization of slurry conditions such as pH amount of surfactant and solid content.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.900-903
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• 2009

An oat gum was extracted from whole seeds of a drought harvested oat (Avena sativa). Oat gum presented a ${\beta}-glucan$ content of 65%(w/w) and an intrinsic viscosity of 141 mL/g. Gelling capability of oat gum at different concentrations was investigated. Gel hardness increased from 0.08 to 0.25 N as the oat gum concentration changed from 5 to 10%(w/v). Whippability, foam stability, emulsion stability, and reduced viscosity of oat gum at different pH were also investigated. Oat gum whippability was maximum at pH 7 (146%), while the higher foam and emulsion stability values were found at pH 9 (88 and 96%, respectively). The gum reduced viscosity increased from 715 to 958 mL/g as the pH changed from 7 to 9. Oat gum shows great potential as a gel forming, thickening, and stabilizing agent.

• YAKHAK HOEJI
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• v.34 no.6
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• pp.415-421
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• 1990

The effects of temperature, pH, light and concentration on the degradation of trimebutine maleate in aqueous solution were investigated on the basis of accelerated stability analysis, and the stabilization of the solution was attempted by addition of several additives. The decomposition of trimebutine maleate in solution followed first-order reaction the was not only accelerated by temperature elevation but also the lower the concentratin the more speeded up the reaction. The decomposition mechanism of trimebtine could be confirmed by hydrolysis of ester bond in the structure. It was assumed trimebutine maleate is so photosensitive that the solution of the drug underwent accelerated decomposition under UV rays. What is more, the degradation of trimebutine solution was supposed to catalyzed by specific acid-base catalysis considered the pH dependence for the hydrolysis of ester, and the solution was most stable over the range of pH 2-2.8 in solution. The additives, citric acid, asparitc acid and glutamic acid, inhibited considerably the decomposition of the drug solution, and these additives might be used as stabilizers in trimebutine maleate solution.

• Journal of Microbiology and Biotechnology
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• v.27 no.3
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• pp.507-513
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• 2017

Bacillus subtilis spores can be used for protein display to engineer protein properties. This method overcomes viability and protein-folding concerns associated with traditional protein display methods. Spores remain viable under extreme conditions and the genotype/phenotype connection remains intact. In addition, the natural sporulation process eliminates protein-folding concerns that are coupled to the target protein traveling through cell membranes. Furthermore, ATP-dependent chaperones are present to assist in protein folding. CotA was optimized as a whole-cell biocatalyst immobilized in an inert matrix of the spore. In general, proteins that are immobilized have advantages in biocatalysis. For example, the protein can be easily removed from the reaction and it is more stable. The aim is to improve the pH stability using spore display. The maximum activity of CotA is between pH 4 and 5 for the substrate ABTS (ABTS = diammonium 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate). However, the activity dramatically decreases at pH 4. The activity is not significantly altered at pH 5. A library of approximately 3,000 clones was screened. A E498G variant was identified to have a half-life of inactivation ($t_{1/2}$) at pH 4 that was 24.8 times greater compared with wt-CotA. In a previous investigation, a CotA library was screened for organic solvent resistance and a T480A mutant was found. Consequently, T480A/E498G-CotA was constructed and the $t_{1/2}$ was 62.1 times greater than wt-CotA. Finally, E498G-CotA and T480A/E498G-CotA yielded 3.7- and 5.3-fold more product than did wt-CotA after recycling the biocatalyst seven times over 42 h.

• Journal of Pharmaceutical Investigation
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• v.28 no.2
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• pp.121-126
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• 1998

The solubility and physicochemical stability of caroverine hydrochloride (CRV), an antispasmodic, in buffered aqueous solutions were studied using a reverse phase high performance liquid chromatography. The solubilty of the drug at pH 2.76-5.40 was similar at the range 31.9-36.2 mg/ml $(34^{circ}C)$, but, at the pH higher than 6.0, markedly decreased. The use of polyethylene glycol 400 as a cosolvent did not increase the solubility at any compositions examined. Moreover. increasing molar concentration of aqueous phosphate buffer from 0 to 0.5 M remarkably decreased the solubility. The degradation of CRY followed the apparent first-order kinetics. The degradation was accelerated with decreasing pH and increasing storage temperature. The half-lives for the degradation of CRY (1.0 mg/ml) at pH 1.28. 4.01 and 5.93 $(45^{\circ}C)$ were 2.8, 31.4 and 124 hr. respectively. The pHs of incubated solutions were to some extent lowered perhaps due to the formation of acidic degradation products. The addition of disodium edetate (0.01%) to the CRY solution (pH 4.95) retarded 2.5 times the degradation rate at $45^{\circ}C$, but the use of sodium bisulfite (0.1%) accelerated 2.9 times the rate. The activation energy for the CRY solution (20 mg/ml. pH 5.4) containing 0.01% EDTA was calculated to be 5.98 kcal/mole. When the solution was stored under nitrogen displacement in ampoule, there was no significant degradation even after 3 months at $40^{\circ}C$, indicating that protection from oxidation by air (oxygen) is essential for the complete stabilization of CRY solution.

• Korean Journal of Food Science and Technology
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• v.25 no.2
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• pp.109-117
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• 1993

To investigate the effects of sodium alginate, gum karaya and gum arabic on the foaming properties of sodium caseinate, surface tension, specific viscosity, turbidity, foaming ability and foam stability of the caseinate solution with added gums were examined. Surface tensions of the 5%(w/v) protein solutions containing gums at pH 7.0 and 8.0 were $43.7{\sim}44.7dyne/cm$ and $43.6{\sim}44.0 dyne/cm$, respectively. Specific viscosities of the solutions with 0.2 and 0.3% sodium alginates were 15.6 and 39.1 at pH 7.0 (control, 2.8), and 12.1 and 8.2 at pH 8.0 (control, 2.6), respectively. Turbidities were $69.5{\sim}74.0$ at pH 7.0 and $68.0{\sim}72.5$ at pH 8.0. The optimum conditions for foaming ability of the solutions were 0.1% conc. and 15 min whipping in addition of sodium alginates; 0.2% conc. and 20 min whipping in gum karaya; 0.1% conc. and 10 min whipping in gum arabic. For foam stability optimal concentrations were 0.3% in sodium alginate and gum karaya at pH 7.0 and 0.2% at pH 8.0. Addition of sodium alginates was most effective to increase foam stability of the solution, but was not effective to increase foaming ability. At same pH, surface tensions and turbidity of the solutions were related to foaming ability and specific viscosities were related to foam stability.

• Journal of Food Hygiene and Safety
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• v.31 no.4
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• pp.304-309
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• 2016

This study was assessed stability of ethanolic extract from Cirsium setidens Nakai that will be applied for development of functional foods and ingredients. We evaluated pectolinarin content, total phenol content and antioxidant activity (DPPH radical scavenging activity and FRAP assay) of ethanolic extract from C. setidens Nakai against various temperature (4, 25 and $50^{\circ}C$) and pH (4.0, 7.0 and 10.0). Our results show that the pectolinarin and total phenol contents in ethanolic extract from Cirsium setidens Nakai slightly reduced during the storage periods. Moreover, the DPPH radical scavenging activity at $4^{\circ}C$ was higher than those of other temperature. Pectolinarin content, total phenol content and DPPH radical scavenging activity of ethanolic extract from Cirsium setidens Nakai at acidic (pH 4.0) and neutral (pH 7.0) pH ranges were higher than at alkaline pH ranges. These results indicate that the optimum storage condition of C. setidens Nakai ethanol extract are temperature $4^{\circ}C$ and pH 4.0-7.0 ranges.