• Applied Biological Chemistry
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• v.34 no.1
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• pp.38-42
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• 1991

Salt-soluble protein contents of green and mature persimmon were 1.5 and 2.0mg/100g-fr. wt., respectively, but that of soft persimmon was 58.9mg/100g-fr. wt.. Protein contents of cell wall increased during maturation but decreased in soft persimmon. The chromatograms of salt-soluble proteins by gel filtration were similar during maturation but those of protein extracted from soft persimmon were different from those of persimmon during maturation. The cell wall protein of persimmon was of two kinds and released during softening.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.05a
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• pp.198-201
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• 2004

To investigate hydrostatic pressure (HP) effect on myofibrillar protein (Mf) extracted from bovine Semitendinosus muscle, Ca- and Mg-ATPase activities to evaluate denaturation of myosin and actin, and soluble protein contents were observed. In Mf treated with 100 MPa for 5 min was not observed denaturation of myosin and actin. In Mf treated with 200 MPa for 5 min, denaturation of myosin and actin were observed but inactivation rate was low (0.0136 $min^{-1}$). Inactivation rate of myosin and actin was dramatically increased above 300 MPa treatment. However denaturation of myosin and actin was not that critical with duration time. By increasing pressure size, the amount of myosin and actin in soluble protein eluted in 20 mM potassium phosphate buffer (pH 7.0) containing 0.6 M NaCl were decreased. SDS-PAGE of soluble protein released from Mf suspension in 0.1 M NaCl buffer (pH 7.0) showed that low molecular weight proteins (15${\sim}$36 KDa) were released by HP treatment above 200 MPa. From the results, denaturation of myosin and actin, and release of light molecule proteins of Mf were observed by HP treatment over 200 MPa.

• Journal of Microbiology and Biotechnology
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• v.25 no.2
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• pp.247-254
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• 2015

In this presentation, I describe the expression and purification of the recombinant liver X receptor β-ligand binding domain proteins in E. coli using a commercially available double cistronic vector, pACYCDuet-1, to express the receptor heterodimer in a single cell as the soluble form. I describe here the expression and characterization of a biologically active heterodimer composed of the liver X receptor β-ligand binding domain and retinoid X receptor α-ligand binding domain. Although many of these proteins were previously seen to be produced in E. coli as insoluble aggregates or "inclusion bodies", I show here that as a form of heterodimer they can be made in soluble forms that are biologically active. This suggests that co-expression of the liver X receptor β-ligand binding domain with its binding partner improves the solubility of the complex and probably assists in their correct folding, thereby functioning as a type of molecular chaperone.

• Archives of Pharmacal Research
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• v.9 no.3
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• pp.157-161
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• 1986

Isolated calf thymus nuclei were in vitro methylated with S- adenosy-L-methyl-$^{14}C$ methionine, and the proteins were fractionated according to their solubilities. Histone fraction ($H_{2}SO_{4}$-soluble fraction) contained approximately 60% total radioactivity incorporated, while "residual protein" which was ($H_{2}SO_{4}$-insoluble contained the remaining radio-activity. The "residual protein" was further fractionated into various acidic proteins, which contained very littel of the radioactivity. However, the protein fraction eluted from DEAE-cellulose with 0.5 N NaOH contained the largest amount of radioactivity. This protein was found to be basic in nature by amino analysis.

• Food Science and Preservation
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• v.8 no.2
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• pp.187-192
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• 2001

Amino acid composition of proteins in Italian millet, Common millet and sorghum were invstigated by HCI hydrolysis method. The optimum condition was obtained by hydrolysis at 110$\^{C}$ for 24hr. As major amino acids from protein hydrolyzate, the content of tyosine, arginine and phebylalanine were 7.06%, 6.79% and 6.44%, respectively. The content of glutamic acid in Common millet, Italian millet and Sorghum were 5.73%, 5.64% and 5.46%, respectively. Glycine content was about 2.93% in three samples. Contents of crude protein and pure protein in Italian millet, Common millet and sorghum were determined by micro-kjeldahl method. Crude protein contents were slightly higher than that of pure protein. Protein content of sorghum was higher than those of Italian millet and Common millet. For SDS-PAGE analysis, Italian millet showed more soluble proteins including 50kDa, 30kDa and smaller proteins than other cereals. In particular, Common millet and Sorghum only solubilized proteins less than 15kDa.

• BMB Reports
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• v.44 no.1
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• pp.22-27
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• 2011

A series of elastin-like proteins, $SKGPG[V(VKG)_3VKVPG]_n$-(ELP1-90)WP (n = 1, 2, 3, and 4), were biosynthesized based on the hydrophobic and lysine linkage domains of tropoelastin. The formation of self-assembled hydrophobic aggregates was monitored in order to determine the influence of cationic segments on phase transition properties as well as the sensitivity to changes in salt and pH. The thermal transition profiles of the proteins fused with only one or two cationic blocks (n = 1 or 2) were similar to that of the counterpart ELP1-90. In contrast, diblock proteins that contain 3 and 4 cationic blocks displayed a triphasic profile and no transition, respectively. Upon increasing the salt concentration and pH, a stimulus-induced phase transition from a soluble conformation to an insoluble aggregate was observed. The effects of cationic segments on the stimuli sensitivity of cationic bimodal ELPs were interpreted in terms of their structural and molecular characteristics.

• The Korean Journal of Mycology
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• v.8 no.3
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• pp.159-166
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• 1980

Aspergillus niger van Tieghem was cultured by the method of submerged and synchronized culture for the study of differentiation. Acid-phenol soluble cell proteins of the fungus were extracted from four stages during development. Those acid-phenol soluble proteins were separated by polyacrylamide gel electrophoresis to determine the protein patterns. A new protein band was observed from the pre-sporulation body, color density of the stained protein bands in four tubes differed according to the differentiation stages. The number of protein bands in 10% gels varied from 18 to 16, 17, and 19 according to the course of spore germination stage, conidiophore stage, phialide maturation stage and sporulation stage.

• International Journal of Industrial Entomology and Biomaterials
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• v.48 no.2
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• pp.86-97
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• 2024

Alkaline- or salt-assisted extractions have been widely used to extract edible insect proteins, however, there is a need for extraction techniques that balance cost-efficient production as well as preserving the protein properties. Mealworm proteins (Tenebrio molitor larvae) were extracted using three different extraction methods-alkali (AMP), salt (SMP), and water (WMP)-and then physicochemical and techno-functional properties were examined. AMP had high yield, protein, and amino acid contents, whereas WMP had high moisture, ash, and fat contents. SDS-PAGE showed a wide range of molecular weights in WMP whereas mostly low molecular weights were observed in AMP and SMP. AMP had poor protein solubilities compared to SMP and WMP across all pHs. AMP had enhanced water-holding capacity and emulsion stability, whereas WMP had improved oil-holding capacity and foaming properties. WMP formed a gel with and without the transglutaminase. The physicochemical and techno-functional properties demonstrated that water-soluble mealworm protein was superior to alkali-and salt-soluble mealworm proteins. Considering the cost efficiency and minimal impact on the environment as well, a cold press juicer could be utilized for mass production of mealworm protein compared to the conventional methods of protein extraction using alkali and salt.

• Food Science of Animal Resources
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• v.31 no.6
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• pp.817-826
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• 2011

The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

• Proceedings of the Zoological Society Korea Conference
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• 1996.04a
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• pp.50.1-50
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• 1996

No Abstract, See Full Text