• Archives of Pharmacal Research
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• v.20 no.6
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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.

• Korean Journal of Food Science and Technology
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• v.28 no.2
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• pp.311-315
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• 1996

Thermal stability of aspartame was investigated as affected by the temperature and pH during heating. The thermal stability study of aspartame heated at $60-100^{\circ}C$ showed that aspartame was degraded more rapidly as the heating temperature increased. Activation energy for thermal degradation was 20.77 kcal/mol. The thermal degradation products, a diketopiperazine (DKP) and ${\alpha}$-aspartylphenylalanine (${\alpha}$-AP), were rapidly increased while the aspartame concentration decreased. The pH change of aspartame solution was rapidly decreased during initial three hours of heating and more significant at high temperature. In the pH range ()』 3-7, aspartame was the most unstable at pH 7 and stable at pH 4. The thermal degradation rate contants were 0.827 at pH 7, 0.286 at pH 6, 0.072 at pH 5 and 0.045 at pH 4 during initial heating at $100^{\circ}C$.

• Journal of the Korean Society of Food Culture
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• v.25 no.6
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• pp.788-794
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• 2010

Camellia sinensis L. (green tea) seed oils were prepared by roasting at $213^{\circ}C$ and pressing (RP), pressing (P), and nhexane extraction (H). The physico-chemical properties of the RP, P, and H samples, including fatty acid composition, color, and sensory characteristics were analyzed. RP, P and H samples were thermally oxidized at $180^{\circ}C$, and oxidative stability was determined by DPPH, CDA, and p-AV at 0, 20, 40, 60, and 80 min. Compared to the P and H samples, RP resulted in significantly higher thermal oxidative stability according to the DPPH, CDA, and p-AV results (p<0.05). The ratio of unsaturated fatty acids to saturated fatty acids among RP, P, and H samples were significantly different (p<0.05). The oleic acid and linoleic acid contents in green tea seed oils were 58 and 23%, respectively. Hunter's color value of lightness (L) for the RP, P, and H samples was not significant. Redness (a) of RP was $3.47{\pm}0.119$ and yellowness (b) of H was $60.10{\pm}2.483$, which were significantly different. Compared to RP samples, H and P samples had the highest color and off-odor values in the sensory evaluation. RP samples showed the highest taste value and were significant overall (p<0.05). The thermal stability of RP extraction was more stable than any other method. Camellia sinensis L. seed oil extracted by RP had better sensory characteristics than other edible oils, including soybean oil, grape seed oil, and extra virgin olive oil.

• KSBB Journal
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• v.13 no.5
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• pp.599-605
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• 1998

Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

• Advanced Composite Materials
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• v.18 no.4
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• pp.351-364
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• 2009

The thermal stability and elevated temperature mechanical properties of $SiC_P$/Al-11.7Fe-1.3V-1.7Si (Al-11.7Fe-1.3V-1.7Si reinforced with SiC particulates) composites sheets prepared by spray deposition (SD) $\rightarrow$ hot pressing $\rightarrow$ rolling process were investigated. The experimental results showed that the composite possessed high ${\sigma}_b$ (elevated temperature tensile strength), for instance, ${\sigma}_b$ was 315.8 MPa, which was tested at $315^{\circ}C$, meanwhile the figure was 232.6 MPa tested at $400^{\circ}C$, and the elongations were 2.5% and 1.4%, respectively. Furthermore, the composite sheets exhibited excellent thermal stability: the hardness showed no significant decline after annealing at $550^{\circ}C$ for 200 h or at $600^{\circ}C$ for 10 h. The good elevated temperature mechanical properties and excellent thermal stability should mainly be attributed to the formation of spherical ${\alpha}-Al_{12}(Fe,\;V)_3Si$ dispersed phase particulates in the aluminum matrix. Furthermore, the addition of SiC particles into the alloy is another important factor, which the following properties are responsible for. The resultant Si of the reaction between Al matrix and SiC particles diffused into Al matrix can stabilize ${\alpha}-Al_{12}(Fe,\;V)_3Si$ dispersed phase; in addition, the interface (Si layer) improved the wettability of Al/$SiC_P$, hence, elevated the bonding between them. Furthermore, the fine $Al_4C_3$ phase also strengthened the matrix as a dispersion-strengthened phase. Meanwhile, load is transferred from Al matrix to SiC particles, which increased the cooling rate of the melt droplets and improved the solution strengthening and dispersion strengthening.

• Korean Journal of Microbiology
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• v.13 no.2
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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.

• The Korean Journal of Food And Nutrition
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• v.20 no.4
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• pp.349-355
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• 2007

Periodate-oxidized soluble starch was reacted with papain at pH 4.0, pH 7.0, and pH 9.7, and an oxidized soluble starch-papain conjugate was produced. When compared with native papain, the specific activity decreased to 60%, in both the modified papain reacted with 0.4% $NaBH_4$ and in the modified papain not reacted with $NaBH_4$. The specific activity decreased to 70% in the modified papains reacted with 1.5% $NaBH_4$ and 4.0% $NaBH_4$, respectively. The reduction by $NaBH_4$ did not have an effect in the thermal stability of either the modified or nonmodified papain. An activity of 54.7% remained in the papain modified at pH 4.0, which was incubated at $80^{\circ}C$ for 40 min. The papains modified at pH 7.0 and pH 9.7 and incubated for 40 min at two different temperatures, respectively, were stable to $60^{\circ}C$, and at $80^{\circ}C$ their activities at 56.3% and 44.1 %, respectively. The modified papain's thermal stability pattern was similar to that of native papain, with no increase in its statbility. In the range of pH $2.0{\sim}13.0$, the stability of the papain modified at pH 4.0 decreased greatly between pH $3.0{\sim}5.0$, but it was similar to the native papain at other pH values. The stability of the papain modified at pH 7.0 showed a similar pattern to the native papain at pH $2.0{\sim}6.0$, while its stability increased when moving into the alkali pH range. The papain modified at pH 9.7 also had increased stability, when moving into the alkali range. The results of Hammerstein milk casein, which was reacted with the papains modified at pH 4.0, pH 7.0, and pH 9.7, respectively, and analyzed by FPLC, showed different peaks according to the different modification pHs, and the greatest peak differences were observed with the modification at pH 9.7.

• Textile Coloration and Finishing
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• v.30 no.4
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• pp.264-274
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• 2018

Immobilization of lysozyme on chitosan non-woven using glutaraldehyde(GA) was investigated. For this, 100 % chitosan non-woven was prepared as novel support for the enzyme immobilization. In addition, free lysozyme activity was examined depending on various pH and temperature by measuring time. Moreover, the optimum immobilization conditions depending on various pH, temperature, immobilization time and lysozyme concentration was evaluated. In addition, thermal stability and storage stability of immobilized lysozyme were measured. The characteristics of immobilized lysozyme was examined by FT-IR, surface morphology, and MTT assay. The results are follows: the optimal immobilization of lysozyme were pH 7.0, $25^{\circ}C$, lysozyme concentration 1.5 mg/ml, immobilization time 240 min. The immobilized lysozyme showed higher thermal stability than the free trypsin. The immobilized lysozyme activity was retained 80 % of its initial activity at $4^{\circ}C$ over 30 days of storage. The lysozyme was immobilized effectively on chitosan non-woven by observation of surface morphology.

• The Korean Journal of Food And Nutrition
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• v.10 no.2
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• pp.241-245
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• 1997

In order to make natural food color from Gardenia, we investigated optimal conditions of color extraction, and thermal stability and light stability of color extracted compared with Yellow-4. In case of ethanol extraction, optimal conditions for color extraction were substrate 10%, 4$0^{\circ}C$, pH 7.0 and 42rs, respectively. In case of water extraction, optimal conditions for color extraction were substrate 10%, 7$0^{\circ}C$, pH 7.0 and 48hrs, respectively. Extraction yield in the optimal conditions was 75% in ethanol and 63% in water. The thermal stability and light stability of Yellow-4 were both upper 98%, but those of Gardenia yellow color were 62 and 90%, respectively.

• Food Science of Animal Resources
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• v.34 no.2
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• pp.207-213
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• 2014

This study investigated the effects of microbial transglutaminase (MTGase) and pH-shift processing on the functional properties of porcine myofibrillar proteins (MP). The pH-shift processing was carried out by decreasing the pH of MP suspension to 3.0, followed by re-adjustment to pH 6.2. The native (CM) and pH-shifted MP (PM) was reacted with and without MTGase, and the gelling and emulsion characteristics were compared. To compare the pH-shifted MTGase-treated MP (PT), deamidation (DM) was conducted by reacting MTGase with MP at pH 3.0. Rigid thermal gel was produced by MTGase-treated native MP (CT) and PT. PM and DM showed the lowest storage modulus (G') at the end of thermal scanning. Both MTGase and pH-shifting produced harder MP gel, and the highest gel strength was obtained in PT. All treatments yielded lower than CM, and CT showed significantly higher yield than PM and DM treatments. For emulsion characteristics, pH-shifting improved the emulsifying ability of MP-stabilized emulsion, while the treatments had lower emulsion stability. PM-stabilized emulsion exhibited the lowest creaming stability among all treatments. The emulsion stability could be improved by the usage of MTGase. The results indicated that pH-shifting combined with MTGase had a potential application to modify or improve functional properties of MP in manufacturing of meat products.