• Molecules and Cells
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• v.26 no.1
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• pp.61-66
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• 2008

Cyclic AMP receptor protein (CRP) is allosterically activated by cAMP and functions as a global transcription regulator in enteric bacteria. Structural information on CRP in the absence of cAMP (apo-CRP) is essential to fully understand its allosteric behavior. In this study we demonstrated interdomain interactions in apo-CRP, using a comparative thermodynamic approach to the intact protein and its isolated domains, which were prepared either by limited proteolysis or using recombinant DNA. Thermal denaturation of the intact apo-CRP, monitored by differential scanning calorimetry, revealed an apparently single cooperative transition with a slight asymmetry. Combined with circular dichroism and fluorescence analysis, the thermal denaturation of apo-CRP could be interpreted as a coupled process involving two individual transitions, each attributable to a structural domain. When isolated individually, both of the domains exhibited significantly altered thermal behavior, thus pointing to the existence of non-covalent interdomain interactions in the intact apo-CRP. These observations suggest that the allosteric conformational change of CRP upon binding to cAMP is achieved by perturbing or modifying pre-existing interdomain interactions. They also underline the effectiveness of a comparative approach using calorimetric and structural probes for studying the thermodynamics of a protein.

• Journal of Korean Ophthalmic Optics Society
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• v.12 no.1
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• pp.9-15
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• 2007

The aim of this study was to find the proper UV-A blocking percentage that could protect the denaturation of ribonuclease A (RNase A), one of protein enzymes in eye, induced by UV-A. RNase A was irradiated at 365 nm for 1, 3, 6, 24, 48, 72, 96 hr and the extent of denaturation was monitored by polyacrylamide gel electrophoresis. Furthermore, it was investigated whether blocking of UV-A by 20, 50, 80 and 99% eyeglass lens could protect the denaturation of RNase A or not. The denaturation of RNase A was induced by only 1 hr UV-A irradiation and the extent of denaturation became severe depending on UV-A irradiation time. The mild denaturation of RNase A induced by irradiation for 1 hr could be sufficiently protected by 20% UV-A blocking lens. When RNase A was irradiated for 3 hr, more that 50% blocking of UV-A needed to prevent the denaturation. Even though 99% UV-A blocking lens was used, the denaturation of RNase A induced by 6 hr irradiation could not be prevented perfectly. However, 99% UV-A blocking lens could dramatically decrease the severe denaturation of RNase A induced by irradiation for 96 hr.

• 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.20 no.2
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• pp.146-151
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• 2000

The objective of this study was to investigate the characteristics on the thermal denaturation of free drip released from pork loin during chilled storage using DSC(differential scanning calorimetry). DSC thermogram of drip released from normal pork(NORD) was characterized by a minor peak and two major peaks with temperature maxima at $61.5^{\circ}C$, $71.7^{\circ}C$ (associated with sarcoplasmic proteins) and $84.3^{\circ}C$ (associated with protein-protein interaction and aggregation). In the denaturation temperature of drip released from PSE pork (PSED), the peak(Tmax) at $59.0^{\circ}C$ was reduced by $2.5^{\circ}C$. When the thermograms were divided into segments correponding to the three peaks, $\Delta$H2 was shown to be reduced by 10% in PSED as compared to NORD. With the decrease in the solubility of sarcoplasmic proteins in PSE muscle, there was a corresponding increase the drip loss during the storage.

• Food Science of Animal Resources
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• v.21 no.3
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• pp.265-271
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• 2001

We investigated changes of immunoglobulin G (IgG) concentrations by heating and drying condition. Also it is performed to group for commercial product by promoting of IgG preservation and reducing of protein denaturation. The result was that content of IgG in colostrum was higher than normal milk. Especially, IgG content of colostrum within 12 hrs after parturition was over 44.67mg/ml and it is 60 times of normal milk. IgG contents was reduced rapidly according as passage of the time. IgG content of the sample heating at 30min at 65$^{\circ}C$ was still a little higher that heating for 10sec at 72$^{\circ}C$. IgG denaturation of heat treatment at 100$^{\circ}C$ for 10sec was lower than at 85$^{\circ}C$ for 30min. We investigated the changes of IgG concentrations of kinds of market milk different with heating processing. This result showed that IgG denaturation ratio by ultra high temperature pasteurization (UHT) was higher than long time low temperature pasteurization (LTLT). On the other hands, IgG content by spray drying was 14.5mg/g and freezing drying was 10.8mg/g. It showed that denaturation of protein content by freezing drying was more than spray drying.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.146-148
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• 2001

The objective of this study was to investigate the behavior of ribonuclease A (RNase) at the water/methylene chloride interface. It was aimed at better understanding the denaturation of proteins upon emulsification. RNase was vulnerable to the interface-induced aggregation reactions that led to formation of water-insoluble aggregates upon emulsification. Biochemical analyses demonstrated that intermolecular covalent linkages might have been involved in the aggregation reactions. The protein instability observed with emulsification was traced to consequences of protein adsorption and conformational rearrangements at the interface. These results indicated that emulsifying aqueous protein solutions in organic solvents should be handled with care, since emulsification could bring denaturation and aggregation to proteins.

• Food Science and Biotechnology
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• v.14 no.1
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• pp.11-15
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• 2005

Dynamic shear moduli of isolated soy protein solutions upon heating were measured to monitor gelation. Onsets of gelation coincide with onset temperatures of denaturation in glycinin and ${\beta}$-conglycinin solutions, whereas in isolated soy proteins, onset of gelation was above denaturation temperature of ${\beta}$-conglycinin with storage modulus increasing in two steps. The first increase in storage modulus of isolated soy proteins occurred at about $78.5^{\circ}C$, while the second increase started at about $93^{\circ}C$. Gel properties of soy protein gels having different proportions of glycinin and ${\beta}$-conglycinin were measured by compression-decompression test. ${\beta}$-conglycinin was responsible for gel elasticity. Glycinin significantly increased hardness, toughness, and fracturability of gels at high heating temperature near $100^{\circ}C$. Results reveal texture of soy protein gels can be controlled by regulating ratio of glycinin to ${\beta}$-conglycinin and heating temperature.

• 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.

• Applied Biological Chemistry
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• v.13 no.1
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• pp.81-85
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• 1970

In this studies, we isolated a kind of protein from Alisma Canaliculatum by the saline extraction. This protein was found to have a strong protective effects on the denaturation of ${\alpha}-chymotrypsin$ in the solution state. The obtained important results during the studies were as follows, 1. This protein was never hydrolyzed by the ${\alpha}-chymotrypsin$. 2. The denaturation of ${\alpha}-chymotrypsin$ was strongly protected by this sample protein. 3. Isoelectric point of this sample was about 4.7. 4. This sample protein was determined as an antigen but very weak antigenicity was indicated on rabbit.

• Korean Journal of Food Science and Technology
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• v.2 no.2
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• pp.49-55
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• 1970

In preparation of textured soybean protein, drying process of the isolated protein affected its gelling property and other related characteristics such as water holding capacity and viscosity. In model systems, denaturation of the protein, as determined in terms of nitrogen solubility index (NSI), was appeared to be a parameter of the gel strength of soybean protein isolate. The gel strength was maximum when the protein was denatured properly during drying process of which the NSI was 43 in this experiment and decreased at either the higher or the lower NSI. It indicated that proper denaturation of the protein during drying operation is advantagous for the preparation of textured soybean protein but not neccesary to make highly undenatured one.