• Korean journal of food and cookery science
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• v.24 no.3
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• pp.304-311
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• 2008

This study examined Jeung-pyun(JP) Retrogradation in samples containing 3% whole protein, 7S protein, or 11S protein(w/w) that were stored at $4^{\circ}C$ for 6, 12, 24 and 72 hr. Rheometery and differential scanning calorimetry(DSC) were used in the analysis. The pH of the dough decreased during the fermentation process, but it increased after steaming. The JP prepared with soybean protein isolate(SPI) had higher pH than the control group. During storage the textural characteristics of the JP showed effects according to the additions of SPI. After 6 hr of storage, the JP samples containing soybean flour, whole protein, 7S protein, and 11S protein had lower hardness valuse. From 4 hr to 12 hr, higher springiness values were found in the samples containing whole protein, 7S protein and 11S protein. At 0 hr, the control group had the highest cohesiveness value, but after 24 hr it presented the lowest value. For gumminess, after 6 hr of storage, the control group offered the lowest value. Whereas after 12 hr of storage the whole protein group showed the highest value, and at 24 hr, the whole protein, 7S protein, and 11S protein groups had higher values. According to the DSC results, the 11S protein group had lower enthalpy values(${\bigtriangleup}H$) suggesting that adding 11S protein to JP might improve starch retrogradation. After 72 hr of storage, the control group had the highest onset temperature($T_{o}$) and peak temperature($T_{p}$) whereas the 7S and 11S protein JP samples had higher conclusion temperatures($T_{c}$). Therefore, based on the different analysis result between the control and treatment groups, the addition of SPI to Jp had effects on retrogradation.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.44 no.4
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• pp.350-354
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• 1999

Soybean varieties derived from Korea are classified into four groups on the basis of their food types such as soybeans for vegetable, sprout, sauce and paste and soybeans with colored seed coat. This study was carried out to know the differences in storage protein concentrations among these four groups. There were differences in storage protein concentrations among four groups. In 7S protein, the $\alpha$'-and $\alpha$-subunit concentrations did not vary among four groups, while a $\beta$-subunit concentration greatly varied. 7S protein concentration was the highest(40.6%) in soybean for sauce and paste and the lowest(37.7%) in soybean for vegetable, while 11S protein concentration was the highest (62.3%) in soybean for vegetable and the lowest (59.4%) in soybean for sauce and paste. In view of the fact that 11S protein has much higher sulfur containing amino acids than 7S protein, it was shown the soybeans for vegetable may have higher nutrition value than other groups.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.35 no.5
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• pp.403-412
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• 1990

Soybean grain, the main source of protein and lipid, has been used for various purposes in our food resources. Therefore, to abtain and supply protein in safety, soybean must be considered as more and more important and it must be made many efforts in breeding for good quality and high protein. Contents of seed protein of the recommeded soybean cultivars in Korea were above 40 persents. Soybean seed protein was divided four fractions by solubility differences. Contents of fraction-albumines, globulines, prolamines and glutelines- were 7.59%, 71.43%, 1.32%, and 9.11% to total protein in Jangyeobkong. The major components of amino acids were glutamic acid, aspartic acid and arginine in order, cystein, methionine, and tyrosine were the minor components in soybean seed protein. Soybean seed protein is constituted mostly of 11s and 7s proteins. Contents of methionine and cystein, sulfur containing amino acid, in 11s protein has already identified higher than 7s protein's The yields of soybean curd were positively correlated with the soluble protein contents of the soybean varieties.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.33 no.s01
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• pp.39-47
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• 1988

Soybean grain is most widely used and soybean crop produces most high protein per area among crops. To meet rapid increase of human population and supply protein in safety. soybean has considered more and more important crop. And it has been emphasizing that high quality and high protein soybean breeding must be made efforts in future. Many papers related to soybean breeding for high quality and protein and soybean protein composition have suggested the problems to do in future. Soybean germplasm collection. classification and conservation should be continuously performed, and it is emphasized that wild type of soybeans (G. soja) be considered to use in breeding for high protein varieties. Selections would be better emphasized in first yield and therefore high yield of protein per area. Selection for high protein would be secondary criterion. High protein lines with high yielding potential could be selection from certain populations, and breeders should consider this phenomenon in procedure of selection. Heritability of protein percent is relatively high and genetic gain of increment of protein percent is large. Soybean protein which is comprised 70 to 90% of globulin is constituted mostly 11S and 7S proteins. Sulfur-containing amino acids, methionine and cysteine, are identified to contain more in 11S protein than 7S protein. High 11S germplasm should be desirable to use in crossing plan, and selection of high ratio of 11S/7S lines be better in development of high quality varieties.

• Archives of Pharmacal Research
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• v.28 no.11
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• pp.1275-1281
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• 2005

The $G_{q/11}$ protein-coupled receptors, such as muscarinic (M1 & M3) receptors, have been shown to regulate the release of a soluble amyloid precursor protein (sAPP$\alpha$) produced from $\alpha$-secretase processing. However, there is no direct evidence for the precise characteristics of G proteins, and the signaling mechanism for the regulation of $G_{q/11}$ protein-coupled receptor mediated sAPP$\alpha$ release is not clearly understood. This study examined whether the muscarinic receptor-mediated release of sAPP$\alpha$ is directly regulated by $G\alpha_{q/11}$ proteins. The HEK293 cells were transiently cotransfected with muscarinic M3 receptors and a dominant-negative minigene construct of the G protein $\alpha$ subunit. The sAPP$\alpha$ release in the media was measured using an antibody specific for sAPP. The sAPP$\alpha$ release enhancement induced by muscarinic receptor stimulation was decreased by a $G_{q/11}$ minigene construct, whereas it was not blocked by a control minigene construct (the G$\alpha$ carboxy peptide in random order, G$\alpha_{q}$R) or $G\alpha_{j}$ constructs. This indicated a direct role of the $G\alpha_{q/11}$ protein in the regulation of muscarinic M3 receptor-mediated sAPP$\alpha$ release. We also investigated whether the transactivation of the epidermal growth factor receptor (EGFR) by a muscarinic agonist could regulate the sAPP$\alpha$ release in SH-SY5Y cells. Pretreatment of a specific EGFR kinase inhibitor, tyrophostin AG1478 (250 nM), blocked the EGF-stimulated sAPP$\alpha$ release, but did not block the oxoM­stimulated sAPP$\alpha$ release. This demonstrated that the transactivation of the EGFR by muscarinic receptor activation was not involved in the muscarinic receptor-mediated sAPP$\alpha$ release.

• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.344-349
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• 1988

Proteolysis of 7S and 11S soy protein-rich fraction(PRF) with commercial proteases(alcalase and pronase) apperently increased protein solubility at pH 5, heat coagulation and calcium tolerence, while decreasing emulsifying capacity and foam stability regardless of the kind of protein and protease used. However, the proteolysis decreased the protein solubility of 7S PRF at pH 6 and 11S PRF at pH 4. The proteolysis of 11S PRF increased oil absorption and foam expansion, while slight decrease or almost no change was noted on 7S PRF. Heat stabilities of the emulsion and kinetic viscosities changed very little by the proteolysis.

• Korean journal of food and cookery science
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• v.23 no.6
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• pp.810-817
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• 2007

The quality properties of Jeung-pyun made with soybean protein isolate(SPI) were investigated. The SPI Jeung-pyun was manufactured using 3% whole protein, 7S protein or 11S protein(w/w). The redness values (a-values) of the Jeung-pyun were negative and the yellowness(b-value) of the control group was significantly lower compared to the other samples. The textural characteristics of the Jeung-pyun were influenced by the additions of SPI. The Jeung-pyuns containing soybean flour, whole protein, 7S and 11S protein had increases in springiness, but decreases in cohesiveness. In the sensory evaluation, overall desirability, sweetness, and moistness were highest in the whole protein group. The control group showed the highest scores for hardness and toughness, and the scores for after-taste and adhesiveness were the highest in the samples made with soybean flour. The 7S and 11S additions showed high scores in terms of color and springiness. In the analyses for consumer acceptance and sensory quality intensity, the whole protein addition had significantly higher scores for general acceptability and the Makgeolli flavor. Hardness was highest for the control group and the Makgeolli flavor was strongest with the soybean flour addition.

• 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.

• BMB Reports
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• v.33 no.2
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• pp.188-192
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• 2000

Recombinant protein G has been utilized in the purification of antibodies from various mammalian species based on the interaction of antibodies with protein G. The interaction between immunoglobulin and protein G may not be restricted to the Fc protion of antibodies, as many different $F(ab)_2$ or Fab fragments can also bind to protein G. I found both FAb $F(ab)_2$ of 145-2C11, a hamster anti-mouse $CD3{\varepsilon}$ antibody, bound to the protein G-sepharose. Interestingly, Fab and $F(ab)_2$ of 145-2C11 did not bind to the protein A-sepharose. The binding of Fab and $F(ab)_2$ of 145-2C11 to protein G provided a useful method to remove proteases, chopped fragments of the Fc region, and other contaminating proteins. The remaining intact antibody in the protease reaction mixture can be removed by using a protein A-sepharose, because the Fab and $F(ab)_2$ portions of 145-2C11 did not bind to protein A-sepharose. The specific binding of Fab and $F(ab)_2$ portions of 145-sC11 to a protein G-sepharose (though not to a protein A-sepharose) and binding of intact 145-2C11 to both protein A- and G-sepharose will be useful in developing an effective purification protocol for Fab and $F(ab)_2$ portions of 145-2C11.

• Journal of the East Asian Society of Dietary Life
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• v.18 no.1
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• pp.1-8
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• 2008

In this study the rheological properties of Jeung-pyun prepared with soybean protein isolate (SPI) were investigated. SPI Jeung-pyun samples were manufactured with 3% whole protein, 7S protein, or 11S protein (w/w). In terms of moisture content the Jeung-pyun samples prepared with soybean flour had greater moisture contents than the control group. With the addition of SPI water binding capacity solubility and swelling power increased. Dough pH decreased during the fermentation, but increased after steaming and the SPI Jeung-pyun samples presented higher pH levels han the control group. Foaming ability was significantly strong in the 7S, 11S and whole protein groups. The surface structures of the 7S, 11S and whole protein Jeung-pyun samples displayed small uniform pores when examined by SEM. Overall, the results suggest that SPI can contribute to quality improvements in Jeung-pyun through effects on dough fermentation.