• Korean Journal of Environmental Agriculture
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• v.27 no.4
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• pp.460-463
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• 2008

The change of glutelin contents in rice grain during the maturity period was investigated to determine optimum rice harvesting time. The glutelin content was increased with increasing time after heading. In this study, eight of glutelin subunits were found. Among the glutelin subunits, 7208-subunit (MW, 35 kD) contents was significantly increased at 65 days after heading compared with 55 and 60 days after heading. 7405-subunit (MW, 50 kD) contents was steadily increased with time after heading. The results showed that at 55th day after heading would be optimum time for harvest to get the low glutelin content of rice grain.

• Korean Journal of Agricultural Science
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• v.24 no.2
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• pp.121-125
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• 1997

A total of 437 landraces of rice from Vietnam were analyzed for total seed protein by SDS-PAGE and phenol reaction. The different types of glutelin $\alpha$ subunits were detected. The level of wx protein with 60kDa molecular weight was divided into 3 groups, corresponding to non-glutinous, intermediate and glutinous starch types. Based on the variation in seed storage protein and wx protein, landraces were classified into 7 groups. Frequency distribution of types A and B of glutelin $\alpha$ subunits changed with the latitude at which rice landraces were collected. Geographical cline for phenol reaction was detected.

• 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 CROP SCIENCE
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• v.51 no.spc1
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• pp.92-102
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• 2006

Abundant proteins often cause problems in proteome study. Glutelin family proteins (hereafter referred to glutelin) are present in rice proteome sample as over-whelming constituents with very high abundance. In order to increase the number of identified proteins in rice proteome study, we developed a newly improved method for sample preparation through the removal of glutelin. When the protein samples from rice seed were extracted by the conventional trichloroacetic acid (TCA) extraction method, glutelin accounts for about 60% of total rice seed proteins in SDS gels. Using our new water extraction method, glutelin consists of only about 10% of total proteins. After analyzing on a two-dimensional gel electrophoresis (2-DE), 937 protein spots were detected using the conventional TCA extraction method. On the other hand, 1240 proteins could be seen using the new water extraction method. The selectivity for non-glutelin and less abundant protein by the water extraction method was also confirmed by ESI-Q/TOF mass spectrometry analysis. Thus, the new water extraction method developed here can be efficiently used to study the proteome analysis of rice storage seed.

• Proceedings of the Botanical Society of Korea Conference
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• 1987.07a
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• pp.261-282
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• 1987

Plants store a significant amount of their nitrogen, sulfur and carbon reserves as storage proteins in seed tissues. The major proteins present in rice seeds are the glutelins. Glutelins are initially synthesized at 4-6 days postanthesis and deposited into protein bodies via Golgi apparatus. Based on nucleic acid sequences and Southern blot analysis, the three isolated glutelin genomic clones were representative members of three gene subfamilies each containing 5 to 8 copies. A comparison of DNA sequences displayed by relevant regions of these genomic clones showed that two subfamilies, represented by clones, Gt1 and Gt2, were closely, related and probably evolved by more recent gene duplication events. The 5' flanking and coding sequences of Gt1 and Gt2 displayed at least 87% homolgy. In contrast, Gt3 showed little or no homolgy in the 5' flanking sequences upstream of the putative CAAT boxes and exhibited significant divergence in all other portions of the gene. Conserved sequences in the 5' flanking regions of these genes were identified and discussed in light of their potential regulatory role. The derived primary sequences of all three glutelin genomic clones showed significant homology to the legume 11S storage proteins indicating a common gene origin. A comparison of the derived glutelin primary sequences showed that mutations were clustered in three peptide regions. One peptide region corresponded to the highly rautable hypervariable region of legume peptide region of legume 11S storage proteins, a potential target area for protein modification. Expression studies indicated that glutelin mRNA transcripts are differentially accumulated during endosperm development. Promoterss of Gt2 and Gt3 were functional as they direct transient expression of chloramphenicol acetyltransferase in cultured plant cell.

• 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.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.35 no.5
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• pp.413-423
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• 1990

Corn proteins have been known as nutritionally poor, being deficient in the essential amino acids. lysine and tryptophan. Improving the quality of protein in the corn grain would be a great benefit to the farmer. This study was conducted to evaluate the variation of the protein content and the protein constitution of the maize germplasms in the Crop Experiment Station in 1989. The average protein content of 101 germplasms was 11.5% with range from 8.0% to 17.3%. Elite hybrid field corns and table corns possessed 9.1-13.9% protein for the dried whole kernel. Major amino acids were glutamic acid and leucine. Lysine and methionine were limited. Varietal differences were observed in the amino acid composition. Qpm, a modified opaque-2 mutant had 1.4-1.7 times higher lysine content than Suwon 19, a dent corn and Suwon SS-21, a sweet corn. Suwon SS-21 had high threonine content. Maize seed protein gave three fractions. an alchol-soluble fraction (zein), an alkali-soluble fraction (glutelin), and a salt-soluble fraction (globulin) by the Osborne method. The zein fraction accounted respectively for 50.7% and 41.7% of the total protein is Suwon 19 and Suwon SS-21. The nonzein fractions increased in percentage of total protein in Qpm kernels. The amino acid composition of zein fraction from three types maize endoperms of dent, sweet and opaque-2 was essentially identical. Zein contained the high contents of glutamic acid and leucine but low content of lysine. The glutelin fractions of three types maize endosperms were mainly similar in overall amino acid composition. The lysine content of glutelin was higher than that of zein. The amino acid composition of globulin fraction was some different from those of zein and glutelin In Qpm it had higher levels of histidine and lysine than both of zein and glutelin. The increased lysine content in Qpm was resulted from changing the proportions of proteins which contained different levels of lysine.

• Korean Journal of Food Science and Technology
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• v.24 no.1
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• pp.1-6
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• 1992

Changes in protein distributiun, eletrophoretic patterns and amino acid composition were investigated during germination of malting barley. Fractionation of the protein complex in ungerminated malting barley resulted in a higher hordein fraction but less glutelin fraction of the protein complex in ungerminated malting barley resulted in a higher hordein fraction but less glutelin fraction as compared to germinated malting barley. As germination proceeded, NPN, globulin and glutelin fractions continued to increase, accmpanied by decreases in albumin and hordein fractions. The electrophoretic pattern of malting barley proteins showed three bands (molecular weight range of $15,000{\sim}41,000$ daltons) in albumin fraction, five bands ($19,000{\sim}61,000$ daltons) in globulin fraction, five bands ($18,000{\sim}56,000$ daltons) in hordein fraction and tour bands ($20,000{\sim}47,000$ daltons) in glutelin fraction, exhibiting quantitative changes in each fraction during germination. Amino acid analysis showed that glutamic acid, histidine, aspartic acid, serine, glycine, valine, alanine and leucine were major amino acids of proteins in malting barley grains. Glutamic acid increased slightly, but other amino acids showed no definite trend as germination proceeded.

• 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.

• 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.