• Food Science and Biotechnology
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• v.17 no.1
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• pp.135-143
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• 2008

The ratio between 11S Sand 7S globulins was greater in large seed size varieties (LSSVs) of soybean than in small seed size varieties (SSSVs) or medium seed size varieties (MSSVs) but did not differ between MSSVs and SSSVs. The cysteine and methionine contents of 11S globulins were greater than those of total seed proteins and 7S globulins. The acidic monoamino monocarboxylic amino acids were the most abundant class of amino acid in soybean seed (27.2%) and soybean curd protein (29.3%). Isolated 7S and 11S fractions were analyzed by HPLC. Of the 12 peaks detected, 4 constituted 64.1% of the proteins of the SSSVs, 65.6% of the proteins of the MSSVs, and 70.5% of the proteins of the LSSVs. The 11S/7S globulin ratio was related to the yield and hardness of soybean curd. The MSSVs had the greatest yield of soybean curd, but the soybean curd hardness of the MSSVs was greater than that of the SSSVs. These results show that the 11S/7S ratio and color of soybean seeds can be used to predict the yield, hardness, and color of soybean curd.

• The Korean Journal of Food And Nutrition
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• v.12 no.2
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• pp.184-190
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• 1999

Soybean protein consists of two major components $\beta$-conglycinin and glycinin which together consti-tute 70% of the total seed storage protein at maturity. $\beta$-Conglycinin is trimeric glycoprotein and for-med by the assembly of various combinations of three subunits $\alpha$,$\alpha$' and $\beta$ which have molecular weig-hts of 69,000, 72,000 and 42,000, respectively. Recently $\beta$-conglycinin was identified as powerful LDL lip-oprotein receptor activation hypercholesterolemia and major allergenic proteins. To investigate these reasons we constructed an expression system of cDNA encoding $\alpha$-subunit of $\beta$-conglycinin in Escherichia coli and purified the expressed protein. The pro-$\beta$-conglycinin synthesized in Escherichia coli BL 21 (DE3)comprised approximately 15% of the total bacterial proteins and the expressed protein are formed sol-uble and trimer such as native protein in Escherichia coli cells. The highly expressed protein was purified to homogeneity by salt precipitation with 20~40 % ammonium sulfate ion-exchange chromatography with Q-sepharose and hydrophobic column chromatography with Butyltoyopearl.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.49 no.4
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• pp.342-348
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• 2004

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the $60\%$ isopropanol extract of soybean(Glycine max [L.] Merr.) seed revealed two abundant proteins with molecular masses of 19 and 10 kDa. Amino acid analysis revealed that the isopropanol-extractable protein fraction was rich in cysteine. Two-dimensional gel electro-phoretic analysis indicated that the 19kDa and 10kDa proteins had pI of 4.2 and 4.0 respectively. Peptide mass fingerprints of trypsin digests of the two proteins obtained using matrix-assisted, laser desorption/ionization-time of flight (MALDI-TOF) mass spectroscopy revealed the 19kDa protein was Kunitz trypsin inhibitor and the 10kDa protein was Bowman-Birk proteinase inhibitor. When resolved under non-denaturing conditions, the isopropanol-extracted proteins inhibited trypsin and chymotrypsin activity. Results presented in this study demonstrate that isopropanol extraction of soybean seed could be used as a simple and rapid method to obtain a protein fraction enriched in Kunitz trypsin and Bowman-Birk proteinase inhibitors. Since proteinase inhibitors are rich in sulfur amino acids and are putative anticarcinogens, this rapid and inexpensive isolation procedure could facilitate efforts in nutrition and cancer research.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.61 no.4
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• pp.227-234
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• 2016

In this study, we analyzed seed storage proteins in order to investigate the main factors related to the eating quality of japonica and tongil-type rice varieties. Sensory evaluation was performed by a trained panel to assess the appearance (color and glossiness), flavor, taste, stickiness, texture, and overall score of nine japonica and three tongil-type rice cultivars. Moreover, the pattern of variation in rice storage proteins was examined by electrophoresis of protein extracts. The electrophoretic pattern of rice proteins showed 16.4 kDa albumin, 26.4 kDa globulin, 34-39 kDa and 21-22 kDa glutelin, and 14.3 kDa prolamin. In terms of storage protein, the varietal differences between japonica and tongil-type rice were found in albumin, globulin, and the ${\alpha}-1$, and ${\alpha}-2$ sub-units of acidic glutelin. Furthermore, the overall sensory evaluation score was observed to be positively correlated with albumin ($0.495^{**}$) and globulin ($0.567^{**}$), and negatively correlated with ${\alpha}-1$ glutelin ($-0.612^{**}$). Therefore, the results indicated that albumin, globulin, and ${\alpha}-1$ glutelin can affect the eating quality of japonica and tongil-type rice varieties, with the latter having lower eating quality than the former.

• Journal of Plant Biology
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• v.29 no.4
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• pp.243-254
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• 1986

The enzyme patterns and the food storage changes in radish (Raphanus sativus L. cv. Taewang) cotyledons during seedling development were studied. The radish seeds were germinated for 8 days at $25^{\circ}C$ under light (7, 000 lux) or dark condition. The lipid and protein contents per seed were 4.3 mg and 2.85 mg respectively. In 8-day-old light-grown seedling, the lipid and protein contents per cotyledon pair were 1.5 mg and 2.08 mg; in 8-day-old dark-grown seedling, they were 0.8 mg and 1.24 mg respectively. The heterotrophic phase of seedlings continued for 3 days after sowing and followed by autotrophic phase (3~6 day) and senescence phase (6~8 day). The food storage function decreased in response to time course. During heterotrophic phase, the activities of glyoxysomal enzymes (malate synthetase, isocitrate lyase, and catalase) were high at 2~3 day. Those patterns were somewhat more prominent in darkness. During the autotrophic phase, the activities of peroxysomal enzymes (glycolate oxidase and catalase) increased at 4~5 day.

• Asian-Australasian Journal of Animal Sciences
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• v.13 no.6
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• pp.861-882
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• 2000

The seed, or grain, of modern cultivars of Lupinus angustifolius, commonly known as Australian sweet lupins (ASL), is an established feed resource for the intensive animal industries of Australia, Japan, Korea and several other countries in Asia and Europe. Since the introduction of ASL to the world marketplace about 25 years ago, researchers in many countries have found them to be a valuable component of the diet of beef and dairy cattle, sheep, pigs, poultry, finfish and crustaceans. The seed of ASL contains ~32% crude protein (CP) (~35% DM basis) and 5% oil. The main storage carbohydrates in the seed are the ${\beta}$-galactans that comprise most of the cell-wall material of the kernel and the cellulose and hemicellulose of the thick seed coats. ASL seeds contain about 40% non-starch polysaccharides (NSP) and a negligible amount of starch. This makes them an excellent ingredient for ruminant diets, as the risk of acidosis is very low. The seed of modern cultivars of domesticated Lupinus species contain negligible amounts of lectins and trypsin inhibitors so they do not require preheating before being used as an ingredient in feeds for monogastric species. They have a high digestibility coefficient for protein, >90% for most species, but a low energy digestibility, ~60%, which is mostly due to the high content of NSP. The low content of methionine (0.22%) and of lysine (1.46%) is typical of the legumes. The lysine availability for pigs is >70%. Lupin kernels contain ~39% CP (~42% DM basis), 6% oil and 30% NSP. They have a higher digestible energy for pigs and finfish and a higher metabolisable energy for poultry than whole seed. Commercial operations rarely achieve complete separation of kernel from hull and it is more likely that the kernel fraction, called splits or meats, will contain ~36% CP. The replacement of soybean meal or peas with ASL in cereal-based diets for most intensively reared animals, birds and fish is possible provided lysine, methionine and digestible energy levels are kept constant. This makes ASL economically competitive in many, but not all, circumstances.

• 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.

• Journal of Plant Biotechnology
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• v.38 no.4
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• pp.263-271
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• 2011

Rice is one of the most important food crops since it is consumed by approximately 60% of the world's population. The most abundant component of rice grain is starch that is an important source of energy. The second abundant component is protein, which is an important protein source for people in many developing countries that rarely take animal protein. However, the rice protein lacks the essential amino acid lysine. Therefore, nutritional improvement in the essential amino acid composition of rice proteins is required. On the other side, rice grain has attracted attention as a diet and health food in developed countries, because its proteins have superior physiological and food processing properties. Thus, nutritional improvements in rice seed proteins by changing amino acid composition or introducing an useful protein or peptide have been studied. This review aims at assessing the current research status of biosynthesis, accumulation, genetic improvement of seed storage proteins by mutation or genetic engineering in rice.

• Journal of Plant Biotechnology
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• v.1 no.1
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• pp.13-19
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• 1999

The visco-elastic properties of gluten are major determinants of the processing properties of doughs. These visco-elastic properties are strongly influenced by the ratio of monomeric and polymeric proteins and the size distribution of the polymeric proteins, which make up the gluten fraction of the dough. Recent studies have revealed that other features, such as the number of the cysteine residues of the HMW-GS, also play an important role in determining the functional characteristics. To modify the processing properties at molecular level, the relationship between the structure of molecules and dough properties has to be understood. In order to explore the relationships between individual proteins and dough properties, we have developed procedures for incorporating bacterially expressed proteins into doughs, and measuring their functional properties in small-scale equipment. A major problem in investigating the structure/function relationships of individual seed storage proteins is to obtain sufficient amounts of pure polypeptides from the complex families of proteins expressed in the endosperm. Therefore, we have established a simplified model system in which we produce specific protein genes through bacterial expression and test their functional properties in smallscale apparatus after incorporation into base flour. An S poor protein gene has been chosen as a template gene. This template gene has been modified using standard recombinant DNA techniques in order to test the effects of varying the number and position of cysteine residues, and the size of the protein. Doughs have been mixed in small scale apparatus and characterized with respect to their polymeric composition and their functional properties, including dough mixing, extensibility and small scale bating. We conclude that dough characteristics can be manipulated in a predictable manner by altering the cysteine residues and the size of high molecular weight glutenins.

• Journal of agriculture & life science
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• v.43 no.5
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• pp.39-42
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• 2009

Soybean is an important sources of plant proteins for human and animal nutrition. The use of soybean proteins has been expanded in the food industry due to their excellent nutritional benefits. But, Soybeans contain allergenic proteins that cause allergies to sensitive individuals. ${\beta}$-conglycinin(7S globulin) and glycinin(11S globulin) are the major components of storage protein in soybean. ${\beta}$-conglycinin consists of three subunits, ${\alpha}^{\prime}$, ${\alpha}$, ${\beta}$ and exhibits poorer nutritional and food processing properties than glycinin. There is a great deal of interest in the development of soybean lines with reduced amounts of ${\beta}$-conglycinin. The objective of this study was to determine the inheritance of ${\alpha}^{\prime}$-subunit protein in 7S globulin. F2 population was developed from the cross of "Jinpumkong2ho"(${\alpha}^{\prime}$-subunit presence) and PI506876(${\alpha}^{\prime}$-subunit absence) parent. Total 98 of F2 seeds were obtained and analyzed for the segregation of ${\alpha}^{\prime}$-subunit protein by SDS-PAGE. Among 98 F2 seeds, 70 F2 seeds showed ${\alpha}^{\prime}$-subunit protein and 28 F2 seeds did not show ${\alpha}^{\prime}$-subunit protein. The segregation ratios of 3 : 1 for presence and absence of ${\alpha}^{\prime}$-subunit protein were observed(${\chi}^2=0.667$, P=0.414). These data indicate that presence and absence of ${\alpha}^{\prime}$-subunit protein is controlled by a single major gene and might be useful for strain selection of 7S protein reduced soybean.