• Journal of Photoscience
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• v.9 no.2
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• pp.293-295
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• 2002

The structural stability of bacteriorhodopsin (bR) solubilized by Triton X-100 (TX-100) was studied by measuring the denaturation kinetics in the dark and under illumination, and compared with the structural stability of bR solubilized by octyl-${\beta}$-glucoside (OG). In the dark, bR solubilized by TX- 100 was more stable than bR solubilized by OG. Under illumination, bR solubilized by TX-100 showed light-induced denaturation in the same manner as bR solubilized by OG. These results in the dark well correlated with the experimental results of the visible CD band. Although solubilized bR in the TX-100 concentration range of 2-50 mM showed almost identical positive CD band and did not denature in the dark at 35$^{\circ}$C, the kinetic constant of the photobleaching increased with the increase of TX-100 concentration. These results suggested that photo-intermediates of solubilized bR are destabilized by TX-100 micelles.

• BMB Reports
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• v.35 no.5
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• pp.472-475
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• 2002

Phaseolus vulgaris phytohemagglutinin L is a homotetrameric-leucoagglutinating seed lectin. Its three-dimensional structure shows similarity with other members of the legume lectin family. The tetrameric form of this lectin is pH dependent. Gel filtration results showed that the protein exists in its dimeric state at pH 2.5 and as a tetramer at pH 7.2. Contrary to earlier reports on legume lectins that possess canonical dimers, thermal denaturation studies show that the refolding of phytohemagglutinin L at neutral pH is irreversible. Differential scanning calorimetry (DSC) was used to study the denaturation of this lectin as a function of pH that ranged from 2.0 to 3.0. The lectin was found to be extremely thermostable with a transition temperature around $82^{\circ}C$ and above $100^{\circ}C$ at pH 2.5 and 7.2, respectively. The ratio of calorimetric to vant Hoff enthalpy could not be calculated because of its irreversible-folding behavior. However, from the DSC data, it was discovered that the protein remains in its compact-folded state, even at pH 2.3, with the onset of denaturation occurring at $60^{\circ}C$.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.4
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• pp.585-590
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• 2002

The effects of a high level of sucrose on the moisture content, water activity, protein denaturation and sensory properties in Chinese-style pork jerky were investigated. The pork jerky with different levels (0, 12, 15, 18 and 21%) of sucrose was prepared. Fifteen frozen boneless pork legs from different animals were used in this trial. Sucrose is a non-reducing disaccharides and would not undergo non-enzymatic browning. Some studies pointed out that sucrose might be hydrolyzed during freezing, dehydration and storage into glucose and fructose, and cause non-enzymatic browning in meat products. The results showed that moisture content and water activity of pork jerky decreased with increase of the level of sucrose. At the same time, shear value was increased due to the reduced moisture content and water activity by osmotic dehydration. However, a higher level of sucrose had a significantly negative effect on protein solubility and extractability of myosin heavy chain of pork jerky due to non-enzymatic browning. From the results of sensory panel tests, the pork jerky with 21% of sucrose seems to be more acceptable by the panelists in hardness, sweetness and overall acceptability.

• Food Science of Animal Resources
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• v.18 no.3
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• pp.209-215
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• 1998

Effects of protein concentration, ionic strength, pH, and temperature range on the heat-induced denaturation of salt soluble protein extracted from spent layer meat were investigated. Viscosity of salt soluble protein heated at 65$^{\circ}C$ for 30 min began to increase sharply above 7 mg/ml of breast protein concentration, and above 21 mg/ml of leg protein concentration, respectively. Both turbidity and viscosity showed the highest value in cooked protein solution with pH 6.0 and 1% NaCl. The turbidity of salt soluble protein started to increase continuously from 40$^{\circ}C$ to 80$^{\circ}C$. The viscosity increased rapidly from 45$^{\circ}C$ to 60$^{\circ}C$ in breast protein, and increased from 50$^{\circ}C$ to 55$^{\circ}C$ in leg protein, respectively, and then kept relatively constant. Breast protein had higher viscosity than leg protein during heat-induced gelation. Therefore, salt soluble protein from spent layer meat was associated with denatured protein (turbidity change) prior to gelation (viscosity change) during heating. Breast protein showed lower thermal transition temperature, and better gel formation than leg protein during heating.

• The Korean Journal of Food And Nutrition
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• v.7 no.4
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• pp.345-352
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• 1994

High protein beverage of cow-soy milk was prepared by mixing the soymilk and commercial homogenized cow milk in the various ratios. Effect of heat treatment, pH and addition of calcium and sucrose was studied on the water-soluble nitrogen of cow-soy milk The heat-treated soymilk at 10$0^{\circ}C$ were centrifuged at the range of 830~29,900xg for 30 min and 11,200xg was found to be proper for determination of the degree of protein denaturation by centrifugal method. When soymilk was heated at 70~10$0^{\circ}C$ for 30~240 min, soluble nitrogen (QA SN) in supernatant of protein was decreased to 78.0~56.8% due to protein denaturation. Most of heat denaturation of protein was found to be occurred during Initial heating 10$0^{\circ}C$ for all mixed cow-soy milk. The sedimentation of SN was maximum at pH 4.0 In the range of pH 3~8. Addition of sucrose affected little on oASN while calcium addition reduced %SN significantly to approx. 55% for soymilk(100%). The effect of Ca was less as the ratio of cow milk increased.

• Fisheries and Aquatic Sciences
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• v.25 no.1
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• pp.31-39
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• 2022

To clarify the factors influencing the physical properties of fish after heat treatments, we investigated changes in the properties of proteins in the dorsal ordinary and dark muscle of yellowtail (Seriola quinqueradiata) heated under different conditions commonly used for the purposes of food hygiene. High-temperature/short-time heating (85℃ for 90 s and 75℃ for 60 s) affected the protein solubility more than low-temperature/long-time heating (63℃ for 30 min). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and differential scanning calorimetry showed that low-temperature/long-time heating reduced the degree of actin denaturation in fish compared with that by other heating conditions. In addition, collagen solubility was enhanced with low-temperature/long-time heating. Therefore, these results suggest that differences in the degree of actin and collagen denaturation are responsible for the enhanced meat tenderness and diminished meat shrinkage, resulting from low-temperature/long-time heating.

• Korean Journal of Food Science and Technology
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• v.21 no.2
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• pp.173-179
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• 1989

The influence of the storage temperature and time after slaughter on the thermal denaturation of PSE porcine muscle protein was studied by differential scanning calorimetry and by measuring the solubility of the sarcoplasmic proteins. In the DSC therodiagram a decrease of the endotherm enthalpy of the myosin plus sarcoplasmic proteins in PSE muscle could be observed with an increase in the storage temperature and time of post mortem. Storage temperature at $20^{\circ}C$ during the first four hours of post mortem resulted in relatively slight denaturation of myosin plus sarcoplasmic proteins in PSE muscle. Storage temperature above $25^{\circ}C$ caused to increase the denaturation of muscle proteins. The minimal drip loss in PSE muscle could be observed, when the muscle was cooled to $2^{\circ}C$ as quickly as possible post mortem. However, when stored for several hours of post morte at a temperature between $32^{\circ}C-38^{\circ}C$, the drip loss reached the level established for PSE muscle. The paleness of PSE muscle could be prevented to some extent by rapid chill to $20^{\circ}C$ post mortem. The more the muscle proteins in the PSE muscle become denatured during the early storage period of post mortem, the more the drip loss increases. With the increase in the denaturation of myosin plus sarcoplasmic proteins in PSE muscle with regard to temperature of post mortem, there was a corresponding decrease in the solubility of the sarcoplasmic proteins in PSE muscle.

• Journal of Korean Ophthalmic Optics Society
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• v.20 no.2
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• pp.237-246
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• 2015

Purpose: The present study was conducted to reveal the correlation of structural denaturation and decrease of enzyme activity when the antioxidative enzymes, superoxide dismutase (SOD) and catalase (CAT) were repeatedly exposed to UV-B, and further investigate whether the denaturation and inactivation of those enzymes can be effectively blocked by using UV-inhibitory RGP lens. Methods: Each enzyme solution was prepared from the standardized SOD and CAT, and repeatedly exposed to UV-B of 312 nm for 30 minutes, 1 hour and 2 hours a day over 1, 2, 3, 4 and 5 days. Structural denaturation of SOD and CAT induced by repeat UV-B irradiation was confirmed by the electrophoretic analysis, and their enzyme activity was determined by the colorimetric assay using the proper assay kit. At that time, the change in structure and activity of the antioxidant enzymes directly exposed to UV-B was compared to the case that UV-B was blocked by UV-inhibitory RGP lens. Results: SOD exposed repeatedly to UV-B showed the polymerization pattern in the electrophoretic analysis when it repeatedly exposed for 30 min a day, however, the change of its activity was less than 10%. On the other hand, CAT repeatedly exposed to UV-B reduced size and density of the electrophoretic band which indicated a structure denaturation, and its activity was significantly decreased. In the case that the repeat exposure time was longer, CAT activity was completely lost even though some enzyme band occurred in the electrphoretic analysis. In addition, the degeneration of CAT due to UV-B irradiation was inhibited to some extent by using RGP lens with a UV-B blocking of 63.7%, however, it was not completely inhibited. Conclusions: From these results, it was revealed that the structural denaturation of antioxidative enzymes was not perfectly correlated with the reduction in enzyme activity according to the type of enzyme. It is recommended to minimize the exposure time to UV when wearing contact lens, or wear the contact lenses having UV blocking rate of the FDA Class I blocker or the sunglasses having equivalent UV-blocking rate for reducing the damage of antioxidative enzymes induced by UV.

• Journal of Photoscience
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• v.9 no.2
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• pp.118-121
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• 2002

A state of bacteriorhodopsin at high temperature was studied by various spectral measurements. The stability measurements indicated that the onset temperature of the denaturation was 70$^{\circ}C$ in the dark and 60$^{\circ}C$ under illumination. The reactivity of hydroxylamine with the Schiff's base also significantly increased in the temperature range between 60 and 70$^{\circ}C$. A spectral band at about 470 nm appeared in the temperature range higher than 60$^{\circ}C$. The circular dichroism spectra in the visible region started to change from a bilobed exiton type to a positive band at about 60$^{\circ}C$, suggesting that the two-dimensional configuration of bacteriorhodopsin molecules changed from crystalline to amorphous. All the measurements suggested a new state between 60 and 70$^{\circ}C$ in which bacteriorhodopsin is stable only in the dark.

• Proceedings of the Korean Society of Near Infrared Spectroscopy Conference
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• 2001.06a
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• pp.1628-1628
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• 2001

Near infrared (NIR) spectroscopy is a powerful technique for non-destructive analysis that can be obtained in a wide range of environments. Recently, NIR measurements have been utilized as probe for quantitative analysis in agricultural, industrial, and medical sciences. In addition, it is also possible to make practical application on NIR for molecular structural analysis. In this work, Fourier transform near infrared (FT-NIR) measurements were carried out to utilize extensively in the relative amounts of different secondary structures were employed, such as Iysozyme, concanavalin A, silk fibroin and so on. Several broad NIR bands due to the protein absorption were observed between 4000 and $5000\;^{-1}$. In order to obtain more structural information from these featureless bands, second derivative and Fourier-self-deconvolution procedures were performed. Significant band separation was observed near the feature at $4610\;^{-1}$ ,. Particularly the peak intensity at $4525\;^{-1}$ shows a characteristic change with thermal denaturation of fibroin. The structural information can be also obtained by mid-IR and CD spectral. Correlation of NIR spectra with protein structure is discussed.