• YAKHAK HOEJI
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• v.42 no.1
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• pp.46-52
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• 1998

Retroviral integrase is required for integration of viral DNA into the host cell chromosome. Human immunodeficiency virus type-1 integrase was partially purified as a part of a fusion protein linked to a maltose-binding protein and characterized in terms of an endonucleolytic activity. The concentration of the fusion protein purified through an amylose column was about 12mg/ml. Indicating that the solubility of the fusion protein is highly increased by the presence of a maltose-binding protein, considering that the integrase protein alone is poorly solubilized. The endonucleolytic activity of the fusion protein was detected at 0.1 to 1.OmM $Mn^{++}$ ion, but not at any concentrations tested of $Mn^{++}$ ion.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.7
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• pp.1120-1126
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• 2007

An iron-fortified whey protein concentrate (Fe-WPC) was prepared by addition of ferric chloride to concentrated whey. A large part of the iron in the Fe-WPC existed as complexes with proteins such as ${\beta}$-lactoglobulin. The bioavailability of iron from Fe-WPC was evaluated using iron-deficient rats, in comparison with heme iron. Rats were separated into a control group and an iron-deficiency group. Rats in the control group were given the standard diet containing ferrous sulfate as the source of iron throughout the experimental feeding period. Rats in the iron-deficiency group were made anemic by feeding on an Fe-deficient diet without any added iron for 3 wk. After the iron-deficiency period, the iron-deficiency group was separated into an Fe-WPC group and a heme iron group fed Fe-WPC and hemin as the sole source of iron, respectively. The hemoglobin content, iron content in liver, hemoglobin regeneration efficiency (HRE) and apparent iron absorption rate were examined when iron-deficient rats were fed either Fe-WPC or hemin as the sole source of iron for 20 d. Hemoglobin content was significantly higher in the rats fed the Fe-WPC diet than in rats fed the hemin diet. HRE in rats fed the Fe-WPC diet was significantly higher than in rats fed the hemin diet. The apparent iron absorption rate in rats fed the Fe-WPC diet tended to be higher than in rats fed the hemin diet (p = 0.054). The solubility of iron in the small intestine of rats at 2.5 h after ingestion of the Fe-WPC diet was approximately twice that of rats fed the hemin diet. These results indicated that the iron bioavailability of Fe-WPC was higher than that of hemin, which seemed due, in part, to the different iron solubility in the intestine.

• Preventive Nutrition and Food Science
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• v.5 no.4
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• pp.200-204
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• 2000

Protein conjugation of curdlan belonging to $\beta$-1, 3-glucan was carried out to improve it surface functionalities. The glucan was mixed with phosvitin, {TEX}$$\alpha$_{s}${/TEX}-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and he resulting powder was incubated at 6$0^{\circ}C$ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. conjugation with unfolding proteins, i.e., phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbmin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the {TEX}$$\alpha$_{s}${/TEX}-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.

• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.665-671
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• 1999

Post mortem bovine muscle. semitendinosus was used to investigate the effects of gamma irradiation on physicochemical properties. The muscle was cut into pieces of 2 cm in thickness and packaged with 2 different methods; vacuum-packaged and air-packaged. The packaged samples were irradiated at designated doses of 0, 1, 3 and 5 kGy by Cobalt-60 irradiator. Muscle protein solubility, purge loss, composition and contents of free amino acids, and shear force were observed during storage at $4^{\circ}C$. We found no significant differences in the purge loss and the contents of free amino acids. Muscle protein solubility slightly increased depending upon the increase of the dose. The decrease of shear force by gamma irradiation was observed. Therefore, it is considered that meat quality can be improved by gamma irradiation.

• Korean journal of food and cookery science
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• v.31 no.3
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• pp.241-247
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• 2015

This study was conducted in order to evaluate emulsion mapping between emulsion stability and moisture content, cooking yield, hardness, protein solubility, apparent viscosity, and overall acceptability of pork or beef emulsion batters. The pork and beef emulsion batters were added to different parts of the meat. The formulations indicating low emulsion stability and high cooking yield were T1 (pork shoulder), T2 (pork ham), and T5 (beef tenderloin) treatments. Low stability, low hardness and protein solubility were also T1 (pork shoulder), T2 (pork ham), and T5 (beef tenderloin) treatments. The Pearson's correlation coefficients show that emulsion stability is negatively correlated with cooking yield (p<0.05), with a value of -0.90, and positively correlated with hardness (p<0.05), and protein solubility (p<0.01) with values of 0.65 and 0.59, respectively. This approach has been found to be particularly useful for highlighting differences among the emulsified properties in emulsion meat products. Therefore, the results obtained with emulsion mapping are useful in the making of new emulsified meat products of the desired quality.

• Journal of Microbiology and Biotechnology
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• v.31 no.12
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• pp.1732-1740
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• 2021

Tobacco etch virus protease (TEVp) is a useful tool for removing fusion tags, but wild-type TEVp is less stable under oxidized redox state. In this work, we introduced and combined C19S, C110S and C130S into TEVp variants containing T17S, L56V, N68D, I77V and S135G to improve protein solubility, and S219V to inhibit self-proteolysis. The solubility and cleavage activity of the constructed variants in Escherichia coli strains including BL21(DE3), BL21(DE3)pLys, Rossetta(DE3) and Origami(DE3) under the same induction conditions were analyzed and compared. The desirable soluble amounts, activity, and oxidative stability were identified to be reluctantly favored in the TEVp. Unlike C19S, C110S and C130S hardly impacted on decreasing protein solubility in the BL21(DE3), but they contributed to improved tolerance to the oxidative redox state in vivo and in vitro. After two fusion proteins were cleaved by purified TEVp protein containing double mutations under the oxidized redox state, the refolded disulfide-rich bovine enterokinase catalytic domain or maize peroxidase with enhanced yields were released from the regenerated amorphous cellulose via affinity absorption of the cellulose-binding module as the affinity tag.

• Food Science and Biotechnology
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• v.16 no.1
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• pp.49-54
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• 2007

The effects of hydrostatic pressure (HP) treatment on the physicochemical, morphological, and textural properties of bovine semitendinosus (ST) muscle were assessed. Based on SDS-PAGE, the decrease in HP-treated ST muscle protein solubility in 0.1 M KCl buffer (pH 7.0) was attributable to a reduction in the levels of sarcoplasmic protein, and the protein solubility decrease observed in 0.6 M KCl buffer (PH 7.0) was attributable to a reduction in the levels of myosin heavy-chain and actin. Scanning electron microscope (SEM) observations showed that muscle fibers became finer and more compact with increasing pressures. The shear force and hardness of ST muscle pressurized to 300 MPa decreased significantly (p<0.05), however samples pressurized at 100 and 500 MPa exhibited a significant increase in both attributes relative to the control sample (p<0.05).

• 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.

• Food Engineering Progress
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• v.22 no.4
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• pp.344-352
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• 2018

The effects of chemical compositions (protein, lipid, and dietary fiber) on the physical properties of dried biji powders were investigated. The raw biji was freeze-dried (control) and hot-air dried (untreated). The untreated biji was further defatted and deproteinated. The prepared biji powders were analyzed for the proximate composition, total dietary fiber (TDF), water absorption index (WAI), water solubility index (WSI), swelling power, solubility (including the quantification of soluble carbohydrate and protein fractions), and final viscosity (using a rapid visco analyzer). Control and untreated biji powders exhibited the similar chemical compositions. The defatted biji possessed higher TDF, although its protein content did not significantly differ for control and untreated ones. The deproteinated biji consisted mainly of TDF. WAI and swelling power increased in the order: deproteinated > defatted > control > untreated biji powders. WSI and solubility increased in the order: control > untreated > defatted > deproteinated biji powders. The similar patterns were observed for soluble carbohydrate and protein fractions. The deproteinated biji revealed the highest viscosity over applied temperatures, while the untreated one was lowest. Overall results suggested that the physical properties of the dried biji powder were reduced by protein and fat, but enhanced by dietary fiber.

• Journal of Microbiology and Biotechnology
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• v.25 no.2
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• pp.280-287
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• 2015

Current influenza vaccines are produced in embryonated chicken eggs. However, egg-based vaccines have various problems. To address these problems, recombinant protein vaccines have been developed as new vaccine candidates. Unfortunately, recombinant proteins frequently encounter aggregation and low stability during their biogenesis. It has been previously demonstrated that recombinantly expressed proteins can be greatly stabilized with high solubility by fusing stabilizing peptide (SP) derived from the C-terminal acidic tail of human synuclein (ATS). To investigate whether SP fusion proteins can induce protective immunity in mice, we produced influenza HA and SP fusion protein using a baculovirus expression system. In in vitro tests, SP-fused recombinant HA1 (SP-rHA1) was shown to be more stable than recombinant HA1 (rHA1). Mice were immunized intramuscularly with baculovirus-expressed rHA1 protein or SP-rHA1 protein ($2{\mu}g/mouse$) formulated with aluminum hydroxide. Antibody responses were determined by ELISA and hemagglutination inhibition assay. We observed that SP-rHA1 immunization elicited HA-specific antibody responses that were comparable to rHA1 immunization. These results indicate that fusion of SP to rHA1 does not negatively affect the immunogenicity of the vaccine candidate. Therefore, it is possible to apply SP fusion technology to develop stable recombinant protein vaccines with high solubility.