• Food Science and Biotechnology
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• v.15 no.1
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• pp.128-132
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• 2006

This study was undertaken to investigate the effect of peptic and chymotryptic hydrolyses of 7S globulin, the major allergen of soybean protein, on its allergenicity, as measured by enzyme linked immunosorbent assay (ELISA), and to identify the allergenic hydrolyzed fragments of 7S globulin using SDS-PAGE. When 7S globulin was hydrolyzed by pepsin, the allergenicity was reduced by over 50%. However, the allergenicity of 7S globulin reduced by peptic hydrolysis was recovered in the sera from 5 out of 10 patients following sequential chymotryptic hydrolysis. Two fragments, with molecular weights 20-25 and 13-16 kDa, among the hydrolysate of 7S globulin by sequential pepsin and chymotrypsin showed reactivity with sera from 10 soybean-allergenic patients. As a result of the theoretical hydrolyses of ${\beta}$-conglycinin, which is a major protein of 7S globulin, it is suggested that the 20-25 kDa fragments were the fragments of the ${\alpha}$-subunit of ${\beta}$'-conglycinin and that the 10-16 kDa fragments were from the ${\alpha}$'-subunit.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.26-32
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• 1977

The multiple 7S globulins composed of two fractions (A and B) in the electrophoresis with Davis' method were isolated at different stages of the soybean seed development. Electrophoresis of their subunits liberated in PAWU solvent [phenol-acetic acid-water (2 : 1 : 1) solution plus 5M urea] yielded 4 major bands. Observation of both the electrophoretic bands of the multiple 7S fractions(7S-A and 7S-B) and those of their subunits was suggestive of a similarity of the subunit pattern between two 7S fractions. The two fractions in multiple 7S globulins were isolated with DEAE-Sephadex A-50 column$(2.0{\sim}100cm)$ chromatography. They were separated into 2 fractions in a linear gradient concentration of 0.28 to 0.40M NaCl with phosphate buffer (pH 7.8) containing 10mM ${\beta}-mercaptoethanol$(ME). The isolated protein was dissociated into subunits with two different solvent systems; in PAWU solvent and in Tris-HCl buffer(pH 8.0) containing 1% sodium dodecyl sulfate (SDS) and 40mM ME. The dissociated subunits were subjected to electrophoresis in PAWU-treated 7.5% acrylamide gel and in 1% SDS-treated 5.6% acrylamide gel. In PAWU gel electrophoresis, total 7S globulin was separated into 5 major bands, two of which were occupied in common by two 7S fractions(7S-A and 7S-B). In SDS gel electrophoresis, total 7S globulin was separated into 7 major bands, three of which were overlapped with the subunit of the two 7S fractions. The above results alluded us to the presence of a common and/or similar subunit between the multiple 7S globulins.

• Korean Journal of Plant Resources
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• v.12 no.3
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• pp.198-203
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• 1999

7S and 11S globulins are two major storage proteins in soybean seed. For improving the quality of soybean seed protein, an increase of 11S/7S ratio would be a desirable objective because 11S globulin contains much more sulfur-containing amino acids than 7S globulin. In this study, six soybean varieties grown at three locations were used for genetic variation analysis of 7S and 11S globulins. It was possible to screen the soybean genotypes having aberrant subunit compositions of the two globulins by a sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). So, heritabilities, genotypic and phenotypic correlations among eight globulin fraction contents of soybean seeds were estimated. The mean value of 7S and 11S globulin fraction contents were 38.9% and 61.1%, respectively, and the ratio of 7S to 11S globulin ranged from 0.58 to 0.74. The high heritability value was found in $\beta$ subunits but the values of acidic and basic subunits were relatively low. Genotypic correlations were higher than the corresponding phenotypic correlations in most of globulin subunit contents. $\beta$ subunits was negatively correlated with $\alpha$ and $\alpha$' subunits among 7S fractions, while no significant correlation between $\alpha$ and $\alpha$' subunits could be found In case of 11S fractions, acidic and basic subunits exhibited no genotypic but negative phenotypic correlation.

• Food Science of Animal Resources
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• v.36 no.5
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• pp.671-678
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• 2016

Fractioning and/or preheating treatment on the rheological properties of myofibrillar protein (MP) gels induced by microbial transglutaminase (MTG) has been reported that they may improve the functional properties. However, the optimum condition was varied depending on the experimental factors. This study was to evaluate the effect of red bean protein isolate (RBPI) on the rheological properties of MP gels mediated by MTG as affected by modifications (fractioning: 7S-globulin of RBPI and/or preheat treatment (pre-heating; 95℃/30 min): pre-heating RBPI or pre-heating/7S-globulin). Cooking yields (CY, %) of MP gels was increased with RBPI (p<0.05), while 7S-globulin decreased the effect of RBPI (p<0.05); however, preheating treatments did not affect the CY (p>0.05). Gel strength of MP was decreased when RBPI or 7S-globulin added, while preheat treatments compensated for the negative effects of those in MP. This effect was entirely reversed by MTG treatment. Although the major band of RBPI disappeared, the preheated 7S globulin band was remained. In scanning electron microscopic (SEM) technique, the appearance of more cross-linked structures were observed when RBPI was prepared with preheating at 95℃ to improve the protein-protein interaction during gel setting of MP mixtures. Thus, the effects of RBPI and 7S-globulin as a substrate, and water and meat binder for MTG-mediated MP gels were confirmed to improve the rheological properties. However, preheat treatment of RBPI should be optimized.

• Preventive Nutrition and Food Science
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• v.2 no.1
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• pp.77-82
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• 1997

The comparison soy protein coagulation by heat-and enzyme-treatment are summarized. The gelation mechanism of glycinin by heating was mainly due to dissociation and aggregation of the basic subunit of 11S globulin. In case of 7S globulin, macro-soluble aggregates may be formed by noncovalent intraction more than 30min at 8$0^{\circ}C$. Whereas, coagulum occured by the microbial enzyme was more minuter than the other Ca-, HCI-coagulum. Heat treatment attacked the basic subunit of 11S globulin and this results agreed very, how-ever, preferred acidic subunit to basic subunit of 11S globulin and attacked the 7S globulin, that could produce coagulum products within 4~5min at $65^{\circ}C$.

• Preventive Nutrition and Food Science
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• v.3 no.2
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• pp.128-132
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• 1998

7S globulin has been isolate from the defatted soybean meal(glycine max,. merill) by Sepharose-6B column chromatography and CM-Sephadex column chromatography. Coagulum of 7S globulin formed at a temperature of $65^{\circ}C$ in microbial enzyme treatment. In order to characterize the structure of the coagulum, three kinds of coagulum (enzyme-, calcium-and acid-induced coagulum)were compared througth the Scanning Electron Microscope(SEM). The network structure was found to be of two levels. First, there was an appearance on the molecular level in the form of strands. Second, there was a denser network with a fine structure.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.4
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• pp.348-352
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• 1994

Soybean seed consists of two major storage protein, the 7S and 11S globulins. For improving the quality of soybean seed protein, an increase of 11S/7S ratio would be a desirable objective because the 11S globulin contains much more the sulfur-containing amino acids than the 7S globulin. In this study, some soybean varieties were used to investigate the analyzing method for 7S and 11S globulins. 7S and 11S globulins couble be fractionated by their different solubilities in tris buffers. Adjusting the pH and tris concentration were major factors affecting the precipitation of the two globulins. And it was possible to screen the soybean genotypes having aberrant subunit compositions of the two globulins by an sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of total soybean proteins. The ratio of 11S to 7S globulin ranged from 1.29 to 1.38. This paper also dealed with the contribution of protein components in soybean seeds to the physical properties of soycurd. It indicated that the soycurd from crude 11S was remarkably harder than that from crude 7S, and springiness and cohesiveness were slightly higher in soycurd having higher proportion of 11S. So, it may concluded that proportion of protein components in soybean seed can be important factor which controls the suitability for soycurd or other foods.

• The Korean Journal of Zoology
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• v.30 no.4
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• pp.371-378
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• 1987

The fractions of serum proteins, the levels of serum immunoglobulins and the positive rate of HBs Ag were investigated in Korean patients with Down's syndrome. Mean concentrations (g/dl) of serum protein, albumin, a1,-globulin fraction, a2-globulin fraction, $\beta$-globulin fraction and Y-globulin fraction were 7.80$\pm$1.44, 3.89$\pm$0.74, 0.26$\pm$0.09, 0.80$\pm$0. 18, 1.00토0.29 and 1.85$\pm$0.64, respectively. Mean concentrations(mg/dl) of IgG, IgA and IgM were 1,682.17$\pm$600.26, 247.39$\pm$180.86 and 170.87$\pm$79.90, respectively. The positive rate of HBs Ag was 21.74% These results revealed higher levels of Y-globulin fraction, IgG and positive rate of HBs Ag in patients with Down's syndrome than in normal population.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.63 no.1
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• pp.25-34
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• 2018

This study was conducted to investigate the germination and proteome profile characteristics of wheat seeds treated under various concentrations of abscisic acid (ABA). After-ripening, the seeds of three wheat cultivars (Baegjoong, Keumkang, and Uri) showing different levels of dormancy were used. Germination index and germination rate of the cultivars was higher than 0.95% and 98%, respectively, and these were not significantly different under 0, 10, 30, and $50{\mu}M$ ABA at 7 d after germination. However, the growth of the shoot and radicle was significantly inhibited at 10, 30, and $50{\mu}M$ ABA compared to that at $0{\mu}M$ ABA. Mean ABA content of the embryos of seeds germinated at 0 and $50{\mu}M$ ABA for 7 d was 0.8 and $269.0ngmg^{-1}DW$, respectively. Proteins extracted from embryos germinated for 4 d were analyzed by two-dimensional gel electrophoresis, and proteins showing a difference of 1.5-fold or greater in their spot volume relative to that of $0{\mu}M$ ABA were identified. The expression of four protein spots increased at $50{\mu}M$ ABA and two protein spots were detected only at $50{\mu}M$ ABA; these six proteins were all identified as globulin types. Conversely, the expression of three protein spots decreased at $50{\mu}M$ ABA and were identified as cytosolic glutamine sysnthetase, isocitrate dehydrogenase, and S-adenosylmethionine synthetase 2. In conclusion, ABA did not inhibit the germination rate regardless of pre-harvest sprouting characteristics of the cultivars. However, the growth of the shoot and radicle was significantly inhibited by ABA, most likely through the down regulation of glutamine, methyl group donor, and polyamines biosynthesis, among others, while accompanied by globulin accumulation in the embryos.

• Journal of Nutrition and Health
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• v.7 no.4
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• pp.33-37
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• 1974

Changes in the concentration of total protein, albumin, ${\alpha}_1-,{\alpha}_2-,{\beta}-,$ and ${\gamma}-globulin$ in Serum from 138 healthy, normal pregnant woman were studied by the method of cellulose-acetate electrophoresis. 1. The concentration of total serum protein decreased gradually during the first 7 month, and showed a tendency to increase thereafter. 2. The concentration of serum albumin showed a steady continuous fall untill term. 3. During pregnancy,${\alpha}_1$ and ${\beta}-globulin$ value rose, ${\gamma}-globulin$ value fell and ${\alpha}_2-globulin$ value showed no significant change.