• KOREAN JOURNAL OF CROP SCIENCE
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• v.59 no.3
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• pp.245-251
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• 2014

Sorghum seed is traditionally used as health supplements and the secondary food mixed with rice in Korea. While the research of reserve protein in sorghum seed have been carried out in many countries used as major food, much less is known about reserve proteins of Korean local sorghum seeds. To obtain protein characteristics in 20 Korean local sorghum seed, quantitative content of reserve protein was determined after fractionation by modified 'Osbone' method and ${\alpha}$-kafirin of prolamin was determined by SDS-PAGE. Mean albumin, globulin, prolamin and glutelin contents based on total seed protein content of 20 Korean local sorghum seed were 6.2%, 0.9%, 57.9% and 35.1%, respectively. Sorghum cultivar with high prolamin were 'Whin-susu', 'Whin-Chalsusu', 'Whanggeum-Chalsusu', and 'Daepungshushu'. Sorghum cultivar with high ${\alpha}$-kafirin were 'Whin-susu', 'Geumsan-Chalsusu', 'Whin-Chalsusu', and 'Jangmok-susu'. Among the 20 varieties, 'Whin-susu' and 'Whin-Chalsusu' were selected as high ${\alpha}$-kafirin and prolamin sorghum cultivar, which showed 64.5 and 71.9% of prolamin contents, respectively.

• Preventive Nutrition and Food Science
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• v.7 no.4
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• pp.437-441
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• 2002

Rice proteins were extracted from brown and milled rice of five varieties: Kwanganbyeo, Daeanbyeo, Daejinbyeo, Surabyeo, Hwaseongbyeo; and their electrophoretic patterns were analyzed by SDS-PAGE. Albumin was extracted with water, globulin with 5% NaCl, prolamin with 70% ethanol, and glutelin with 0.2 M sodium borate buffer (pH 10.0) containing 0.5% SDS, 0.6% $\beta$-mercaptoethanol. The ratios of albumin : globulin : prolamin : glutelin in the brown rice were 10.8~14.1 : 12.4~16.4 : 3.6~5.3 : 68.6~72.8, and in milled rice were 4.4~5.6 : 10.6~12.0 : 3.9~5.4 : 75.7~79.8. In albumin seven major bands were observed with molecular weights ranging from 14.g~96.8 kDa, in globulin four bands with molecular weights in the range of 14.4~56.9 kDa, prolamin had only one band with a molecular weight of 14.4 kDa, and glutelin had four bands with molecular weights of 14.4 ~ 57.4 kDa. There were no differences in electrophoretic patterns between rice varieties or between brown and milled rice.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.3
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• pp.274-279
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• 1985

Proximate compositions, minerals and protein fractions of the roots of cultured and wild Codonopsis lanceolata of different age groups were examined as the basic research for the study of their source of processed foods. The most abundant proximate composition of the roots of C. lanceolata was observed to be total sugars and next come crude protein, crude fiber, crude fat and ash in descending order irrespective of cultured and wild ones. The richest mineral contained in the roots was noticed to be K and followed by Mg and Ca. Generally increased tendency of crude protein, fat, ash, K, Mg, Ca, Mn, Zn, Cu and P contents were observed with older roots, however, decreased total sugars and Fe content. Lead and cadmium content was far bellow the authorized tolerance limits. The quantitative fractionation of the protein of the roots ranked albumin the highest content, followed by globuin, prolamin and glutelin. Decreased albumin content was observed with the older age roots, while increased globulin, prolamin and glutelin content. The minimum solubility of the soluble protein of the roots was found to be at pH 4.0 and maximum, at pH 10.0. Disc gel electrophoresis of the soluble protein of C. lanceolata roots showed almost similar patterns and numbers of bands. The molecular weight for main band protein was estimated to be about 90,000.

• Applied Biological Chemistry
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• v.26 no.1
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• pp.65-72
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• 1983

The composition of four rice protein groups is greatly affected by the extraction conditions. The extraction amounts of albumins and glubulines primarily depended on the temperature rather than the method of extraction. The total amount of glutelins, the major components of rice storage proteins, could be extracted by a successive extraction processes, extraction with 0.5% SDS-0.1M borate buffer(pH 8.3) followed by extraction with 0.5% SDS-0.6% ${\beta}-mercaptoethanol-0.1M$ borate buffer(pH 8.3). The extracted amounts of glutelin with these solvents were 54.1 and 45% respectively. The further purification of SDS soluble glutelins was achieved by Sephadex G-150 gel column chromatography. The molecular weight of the components in four protein groups has been estimated by SDS-polyacrylamide gel electrophoresis with or without ${\beta}-mercaptoethanol.$ The comparison of albumins and globulins by starch gel electrophoresis at pH 3.1 permitted us to identify seven rice varieties. However, at pH 8.95, the specific bands for Japonica type rice varieties were observed.

• Applied Biological Chemistry
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• v.23 no.1
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• pp.14-22
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• 1980

White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride tinder the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands were found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.

• Journal of the Korean Society of Food Science and Nutrition
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• v.15 no.2
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• pp.152-157
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• 1986

Changes in protein, amino acids composition and protein activity of native Meju were investigated at various time intervals over 6 weeks of fermentation by using, gel filtration, and amino acid analyzer. From the quantitative fractionation of native Meju proteins, albumin content (36.4%) was the highest at 4 weeks. During Meju fermentation, albumin increased gradually but glutelin decreased up to 4 weeks. Globulin and prolamin content did not change substantiantiall. When albumin was fractionated by Sephadex G-200, two main peaks were fractionated and a new peak appeared after 4 weeks. Its molecular weight was extimated to be 66,000 by the gel filtration method. Amino acid composition of albumin in native Meju appeared to be 17 kinds. Glutamic acid content (87.98-317.10) were the highest, followed by aspartic acid and glycine. The proleolytic enzyme activity increased when the native Meju was fermented and marked the maximum value at 4 week.

• Journal of Plant Biotechnology
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• v.38 no.2
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• pp.176-185
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• 2011

Rice is one of the most important crop in the world, in particular for food resources. With its small genome size of 383 Mb, the Oryza sativa is a model plant for genome research. Indeed, it's grain provides human with a source of carbohydrates and proteins. Rice grain has relatively low protein contents (around 8%) compared to other legume seeds (around 40%). Osborne classified seed proteins into water soluble albumin, salt soluble globulin, alcohol soluble prolamin and acidic/alkaline solution soluble glutelin. Glutelin and prolamin are the major storage proteins in rice. For the gene expression study of seed storage proteins, we analyzed 33,192 EST clones at immature stages in a rice cultivar (Oryza sativa L. cv. 'Ilpum'). Based on the expression analysis, we cloned 11 glutelin genes and figured out the 8 genes are located on Chromosome 2. The expression of glutelin genes appears to be about 28.2% of total level in immature seeds. Interestingly, glu-04 is duplicated as inverted sequences on the same chromosomes as far 4.5 kb. Our results indicate that glutelin genes, evolutionarily, were replicated on the chromosome and thus expressed as specific manners. In a whole protein composition analysis, glu05 (type B7) contains the highest lysin contents (4.51%) among the 11 rice glutelin genes. It will be an interesting future work to increase lysin contents by the gene overexpressor strategy with the aim of improved diet nutritionally fortified.

• Korean Journal of Food Science and Technology
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• v.15 no.4
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• pp.370-378
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• 1983

Changes of protein and amino acids composition in improvement-Meju inoculated with Aspergillus oryzae were emamined at various time intervals over 6-day test period. To investigate those changes systematically, Disc gel electrophoresis, gel fiteration and amino acid analyzer were used. Following results were obtained; 1. Nitrogen solubility of the soybean meal in $Na_{2}SO_{4},\;MgSO_{4},\;Na_{2}CO_{3},\;NaCl\;and\;Na_{2}HPO_{4}$ solutions of various concetrations were determinated. The salt soluble protein of soybean meal was highly dispersible on 0.4M $Na_{2}SO_{4}$ solution and the extractability of protein was 33%. 2. From the quantitative fractionation of soybean proteins, albumin content (46.0%) was highest followed by globulin (33.9%), glutelin (19.5%) and prolamin (2.4%). During Meju incubation period, albumin and prolamin increased gradually but glutelin decreased. Globulin content was not changed substantially. 3. When albumin was fractionated by Sephadex G-200, the following results were obtained. Soybean albumin showed fraction which was reduced to 3 fraction at 0-day of incubation. The number of fraction, however increased to 8 after 6-day of incubation. 4. Amino acids of albumin in soybean and Meju appeared to be 17 kinds. Glutamic acid and aspartic acid were the highest. In amino acid composition of cooked soybean albumin, arginine, aspartic acid, glutamic acid and glycine remained higher than those of Meju throughout incubation period. 5. The major fraction of albumins from soybean and Meju fractionated by Sephadex G-200 showed 17 kinds of amino acid. Aspartic acid and glutamic acid were the highest. During Meju incubation period, the change of amino acid composition was investigated; threonine, serine, lysine, histidine, alanine, isoleucine, leucine, phenylalanine and $NH_3$ was increased gradually, the others decreased. 6. According to the electrophoretic pattern, soybean protein showed 13 bands which decreased to 3-after cooking. During incubation, those bands increased gradually to 10 bands after 6-days.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.6
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• pp.701-705
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• 1992

The effect of different boiling methods(with distilled water, 1% salt added water and 1% sodium bicarbonate added water) on the physicochemical properties of Su Ri Chwi (Synurus palmatopinnonatifidus var. indivisus KITAM.) were investigated. The addition of 1% sodium bicarbonate (baking soda) to the boiling water resulted in an increase in the pH of effluent. The green value of cooked Su Ri Chwi was simillar to the raw material. Su Ri Chwi cooked in 1% sodium bicarbonate added for 10minutes retained higher chlorophyll and vitamin C contents than those of Su Ri Chwi treated in distilled water and 1% salt water for 30minutes. 70% of the water-soluble proteins in raw Su Ri Chwi was albumin. However, albumin was decreased by the method used. The contents of glutelin, globulin, and prolamin were increased by the cooking, vice versa. The contents of NDF, ADF, cellulose, and lignin were decreased regardless of the method used, on the other hand, the content of hemicellulose was increased.

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.06a
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• pp.86-86
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• 2017

Prolamins are the main seed storage proteins in cereals. Gluten proteins seem to be prolamins because their primary structure have the meaningful quantity of proline and glutamine amino acid residues. Gluten proteins are found in crops such as wheat (Triticum aestivum), barley (Hordeum vulgare), and rye (Secale cereale) which are major food crops in the Triticeae tribe. Glutenin and gliadin, hordein, and secalin are typical gluten proteins found in wheat, barley, and rye, respectively. Gluten affect grain quality so that many researches, such as isolation or characterization of their genes, have been carried out. To improve the quality of grains in the Triticeae tribe, it is necessary to understand the relationship within their gluten proteins and their evolutionary changes. The sequences of nucleotides and amino acids of gluten protein including glutenins, gliadins, hordeins, and secalins were retrieved from NCBI (https://www.ncbi.nlm.nih.gov/) and Uniprot (http://www.uniprot.org/). The sequence analysis and the phylogenetic analysis of gluten proteins were performed with various website tools. The results demonstrated that gluten proteins were grouped with their homology and were mostly corresponded with the previous reports. However, some genes were moved, duplicated, or disappeared as evolutionary process. The obtained data will encourage the breeding programs of wheat, barley, rye, and other crops in the Triticeae tribe.