• Journal of Ginseng Research
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• v.22 no.3
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• pp.168-172
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• 1998

Systematic electrophoretic analysis of alcohol-soluble proteins and salt-soluble proteins of 247 Panax ginseng (P.g) and Panax quinquefolium (P.q) germplasms seed was carried out on an improved lactate-polyacrylamide gel electrophoresis, a method with high resolving power, good reproducibility and stability. The electrophoregrams of proteins, according to their migration rate, were classified into four groups such as ${\alpha}$, ${\beta}$, ${\gamma}$ and $\omega$ for the alcohol-soluble proteins and three such as I, II and III for the salt-soluble ones. Panax ginseng or Panax quinquefolium had their own unique band pattern distinguishable from each other, regarding as their specific "fingerprint". In this study, 3 of 168 (1.8%) P.g germplasms and 1 of 79 (1.3%) P.q germplasms had their own unique band pattern, showing that P.g and P.q germplasms have poor genetic diversity in species. The band patterns of dry seed and stratified seed (embryo rate=60%) were basically the same. The band number of the F, hybrid of p.gx p.q was exactly equivalent to the number of the common bands plus the specific bands of the two parents, indicating that the difference of band patterns was a genetic trait con- trolled by the nuclear genes. The electrophoregram of F1 of P.g x P.q could be predicted by that of the two parents and the band pattern of the F1 hybrids could be demnonstrated by that of the mixed seed extract from the two parents.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.889-894
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• 2009

Barley proteins are expected to have unique functional properties due to their high content of alcohol soluble protein, hordein. Since the barley proteins obtained by conventional isoelectric precipitation method cannot represent hordein fraction, barley proteins were fractionated to albumin, globulin, glutelin, and hordein with respect to extraction solvents. Functional properties and film-forming properties of solubility-fractionated barley proteins were investigated to explore their potential for human food ingredient and industrial usage. The 100 g of total barley protein comprised 5 g albumin, 23 g globulin, 45 g glutelin, and 27 g hordein. Water-binding capacities of barley protein isolates ranged from 140-183 mL water/100 g solid. Hordein showed the highest oil absorption capacity (136 mL oil/100 g), and glutelin showed the highest gelation property among the fractionated proteins. In general, the barley protein fractions formed brittle and weak films as indicated by low tensile strength (TS) and percent elongation at break (E) values. The salt-soluble globulin fraction produced film with the lowest TS value. Although films made from glutelin and hordein were dark-colored and had lower E values, they could be used as excellent barriers against water transmission.

• Microbiology and Biotechnology Letters
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• v.23 no.3
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• pp.316-321
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• 1995

Some properties of $\beta$-1, 3-glucan synthase system in Saccharamyces cerevisiae were investigated. By extraction with detergent and salt, the membrane preparations could be dissociated into two components, one soluble, the other still membrane bound. Both components, in addition to GTP, were necessary for the activity of $\beta$-1, 3-glucan synthase like other fungi. The protective effect of guanosine nucleotides on the soluble factor pointed to the possibility that this fraction contained a GTP-binding protein. Addition of increasing amounts of soluble factor to a constant amount of insoluble catalytic factor, vice versa, gave rise to a saturation curve. These results, including different types of evidence, indicate that the soluble factor and the catalytic factor form a complex.

• Journal of Applied Biological Chemistry
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• v.60 no.1
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• pp.55-59
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• 2017

Although wheat is a common staple food in the world, some people suffer from a variety of wheat allergies. For example, wheat-dependent exercise-induced anaphylaxis is induced in the gastrointestinal tract by wheat proteins. Relatively high molecular weight proteins that are salt-insoluble induce many wheat allergies. In the present study, we investigated the induction of an allergy response using crude wheat proteins, which are relatively low molecular weight, salt-soluble proteins. The crude antigen used in this study was extracted using phosphate buffered saline. When the antigen extracts from various wheat cultivars were orally administered, differentiable degrees of allergy responses were observed as measured by serum IgE and histamine secretion compared to the control. Serum IgE levels increased following administration of three of the wheat extracts. This evidence suggests that a combination of salt-soluble wheat proteins could be antigens for the induction of various allergy responses.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.6
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• pp.395-401
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• 2001

Crystallins are a family of water-soluble proteins that constitute up to 90% of the wa-ter-soluble proteins in mammalian eye lenses, We present in this paper an alternative purification method for these proteins using polyethylene glycol/dextran aqueous two-phase extraction. Un-der the appropriate conditions, we were able to recover the γ-crystallin fraction essentially free of the remaining proteins. High concentrations of salt at a neutral pH maximize the recovery of γ-crystallins in the top phase and minimize the contamination by the other proteins present in the lenses. The proposed protocol decreases the separation time by about 50%. The complex partition behavior observed for these proteins reflects a delicate balance between protein/phase-forming species(various polymers and salts) and protein interactions. This is evidenced, in part, by the role played by the largest proteins in this group as a "pseudo"phase-forming species.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.5 no.1
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• pp.29-38
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• 1972

The protein composition of abalone muscle was estimated with the following result: on a series of samples analyzed, water-soluble protein, $19\~22\%$, salt-soluble protein, $27\~39\%$: alkali-soluble protein, $20\~26\%$ : and stroma $20\~28\%$ : respectively. It was demonstrated by ultracentrifugal analysis that approximately $65\%$ of the salt-soluble protein is accounted for by paramyosin, $30\%$ by actomyosin, and $5\%$ by myosin, respectively. The ultracentrifugally homogenous paramyosin was prepared by BAILEY's ethanol-dried method. It showed a $S^{\circ}\;_{20,\;{\omega}$ of 3.14s, and was completely salted in with KCl beyond $0.35{\mu}$. The intrinsic viscosity at $25^{\circ}C$ was estimated at 3.1. The paramyosin is rich in several amino acids such as arginine, aspartic acid, glutamic acid, etc., and lacking of both proline and tryptophane, in rough accord with other paramyosins reported. The abalone paramyosin did not show ATPase activity over a pH range of 5 to 9,5 even in the presence of Ca++ or Mg++. So was the case with the paramyosin specimen prepared by BAILEY's wet-extraction method.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.18 no.5
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• pp.409-416
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• 1985

In previous paper (Lee et al., 1983) processing method of sardine meat "surimi" was described as a part of the wort to develop new types of ready-to-cook food materials with dark fleshed fishes. As the other part of the work, processing of low salt mackerel fillet was investigated, in this paper, in which fresh mackerel was filleted, salted in brine or with dry salt for an adequate time until the expected salt concentration reached, washed, air dried (3 m/sec, 15 to $20^{\circ}C$), and finally packed individually in K-flex film bag by vacuum or $N_2$ gas substitution. Salting time and salt concentration of brine was decided by the salt level penetrated into the fillet. As the final salt level was fixed to 4 to $5\%$, salting for 20 hours with $10\%$ dry salt or in $15\%$ brine at $5^{\circ}C$ was enough to get that level of salt. If the final salt level was set 5 to $6\%$, salting for 20-24 hours with $15\%$ dry salt or in $20\%$ brine was adequate. Salt penetration, however, was not much influenced by salting method and temperature. Changes in VBN and salt soluble protein occurred more rapidly in cases of salting with dry salt at $20^{\circ}C$ than salted in brine at $5^{\circ}C$, although it was not significant in the period of 20 to 24 hours. Oxidation of lipid and histamine formation during salting at $20^{\circ}C$ could not be neglected if it was delayed loger than 25 hours. Insolubilizing the salt soluble proteins during the storage of salted fillet occurred rapidly regardless of storage temperature. Browning and histamine formation, however, was depended on temperature and packing condition. In case of air pack, deterioration by browning and rancid was deeply developed but not the case for the packs by vacuum or $N_2$ gas substitution. The shelf-life of the salted mackerel fillet based on panel scores of brown color and rancidity, appeared 21 days for the air packed, and more than 30 days for vacunm or $N_2$ gas packed fillet at $20^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.12
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• pp.1839-1845
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• 2010

This study was conducted to evaluate the effects of salt soluble protein extracts from anchovy (ASSPE) on sausage during storage at $10^{\circ}C$. Sausages were produced containing 5 and 10% ASSPE. Sausages containing ASSPE showed no significant differences in emulsion stability, color, pH, moisture, viable cell count, and VBN compared to the control. The hardness significantly increased with the addition of ASSPE, and sausages containing 5% ASSPE were the highest in gumminess. In the sensory evaluation, sausages containing 5% ASSPE had the highest score in appearance and springiness. In conclusion, the addition of ASSPE in sausage had no effects on storage characteristics, but had a good effect on improvement of quality and sensory characteristics. Especially, 5% ASSPE sausage had good texture and high sensory characteristics due to increased binding capacity. These results suggest that 5% ASSPE may improve the quality and sensory characteristics of sausage.

• Proceedings of the Korean Society of Crop Science Conference
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• 2023.04a
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• pp.156-156
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• 2023

Salinity is a major abiotic stress that limits rice productivity in many regions of the world. In order to develop salt stress tolerant rice plants, genetic engineering is a promising approach. We characterized the molecular function of rice C3H2C3 as a really interesting new gene (RING). Oryza sativa RING finger protein H2-3 (OsRFPH2-3) was highly expressed in 100 mM NaCl. To identify the localization of OsRFPH2-3, we fused vectors that include C-terminal GFP protein (35S;;OsRFPH2-3-GFP). OsRFPH2-3 was expressed in the nucleus in rice protoplasts. An in vitro ubiquitin assay demonstrated that OsRFPH2-3 possessed E3-ubiquitin ligase activity. However, the mutated OsRFPH2-3 were not possessed any E3-ubiquitin ligase activity. Under salinity conditions, OsRFPH2-3-overexpressing plants exhibited higher chlorophyll, proline, SOD, POD, CAT, and soluble sugar contents and lower H₂O₂ accumulation than wild-type plants, supporting transgenic plants with enhanced salinity tolerance phenotypes. OsRFPH2-3-overexpressing plants exhibited low Na+ accumulation and Na+/K+ ratios in their roots. Theses results suggest that overexpression of OsRFPH2-3 can make plant insensitivity about salinity conditions.

• The Korean Journal of Food And Nutrition
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• v.11 no.4
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• pp.409-415
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• 1998

This study was carried out to investigate the effects of freezing temperature on quality of vacuum packaging freezed beef. In case of thaw drip loss, the freezing of -3$^{\circ}C$ and -20$^{\circ}C$ were 5.23% and 5.17% to 60 days respectively, were increased significantly during freezing. The cooking loss of water bath and pan were increased significantly during freezing than the beginning of freezing, but were no different between -3$^{\circ}C$ and -20$^{\circ}C$. The salt soluble protein extractability was decreased during freezing, the -20$^{\circ}C$ freezing was higher than -3$^{\circ}C$freezing. The water soluble protein extractability was increased during freezing higher than during freezing. The myoglobin denatured percentage of the -3$^{\circ}C$ freezing was higher than -20$^{\circ}C$ freezing, the 15 days storage of -3$^{\circ}C$ freezing was highest to 96%. The shear force value was not change during freezing, the myofibrillar fragmentation index during freezing was higher than the beginning of freezing, but was not change during freezing. The pH was decreased to freezing 45 days, after that increased.