• KOREAN JOURNAL OF CROP SCIENCE
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• v.49 no.3
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• pp.256-260
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• 2004

A major challenge facing those involved in the testing of new plant varieties for distinctness, uniformity and stability (DUS) is the need to compare new varieties against all those of common knowlege (reference varieties). One possible approach would be to group new (candidate) varieties and reference varieties using descriptions stored in databases prior to further of official test. testing. This study was carried out to manage a reference variety collection by databasing of hordein profiling. For this purpose, hordein subunits of the 48 National list barley (Hordeum vulgare L) cultivars were analysed. Total 22 of clear scorable hordein subunits were identified from D-subunit to B-subunit region and fifteen different hordein polypeptide patterns were obtained. Based on hordein subunit band pattern, UPGMA cluster analysis was conducted. Forty-eight cultivars were separated into three groups and genetic distance of cluster ranging from 0.55 to 1.00. Hordein subunits have a potential of selecting similar varieties compared with candidate varieties by controlling reference variety collection and playing an important complemental role in cultivar distinctness.

• Applied Biological Chemistry
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• v.29 no.1
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• pp.57-61
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• 1986

Total protein from 4 barley varieties(Olbori, Young San-bori, Sacheon 6, and Suwon 228) was separated into albumin, globulin hordein and glutelin fractions by the Osborne method and tile modified Osborne method in a previous report. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) for the protein fractions revealed that there was a little difference in the polypeptide composition of each fraction among four varieties. The comparision of hordeins and hordein-Is by polyacrylamide gel electrophoresis at pH 3.0 showed a marked difference among the varieties. Hordein-I contained a high level of glutamic acid and proline and low level of lysine. And (here was little difference in amino acid composition of hordein-Is which were extracted from the 4 varieties.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.46 no.2
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• pp.100-105
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• 2001

One-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (1D SDS-PAGE) was used to determine whether it would provide improved resolving power of hordein proteins concomitant with improved identification of Korean barley cultivars and germplams. This system gave rapid and reproducible separations of hordein polypeptides. Total fourteen of clear and easily scorable subunits were identified in Korean barley cultivars and germplasms and their polymorphic constitutions could provide biochemical genetic information in progeny analysis and endosperm quality improvement in barley breeding programs. Each hordein polypeptides residing in B, C, and D hordein pattern designations were scored to prepare a cultivar catalogue of protein patterns. On the basis of this character, 7 hordein polypeptide patterns were constructed from 108 barley cultivars and experimental lines. The molecular weight of hordein subunits in Korean barley cultivars and experimental lines varied in the range of 98 to 48 kDa. In contrast, less polymorphic hordein polypeptides were found in the low protein barley lines including malting barleys than those found in Korean barley cultivars and experimental lines.

• 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.66 no.4
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• pp.326-338
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• 2021

Ultra-performance liquid chromatography (UPLC) was used to assess the hordein protein fraction of malting barley. C-hordeins (barley prolamins) were extracted with 70% ethanol (EtOH) and 55% isopropyl alcohol (IPA, 2-propanol), and B-hordeins were extracted with the same alcohols in 1.0% dithiothreitol (DTT). High molecular weight (HMW) prolamins (D-hordeins) were extracted with 50% IPA with 1M Tris-HCl (pH 8.0). The same protein patterns were observed in both the experimental extraction solutions (EtOH and IPA). However, the patterns of hordein, extracted with EtOH and IPA containing 1.0% DTT, differed slightly. C- and B-hordeins extracted from those solutions were analyzed. Twenty-six malting barley varieties developed in Korea were analyzed using UPLC. The varieties were divided into seven groups according to hordein patterns of retention time 16 min to 18 min, and 20 varieties showed unique patterns.

• Proceedings of the Korean Society of Crop Science Conference
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• 2000.04a
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• pp.392-393
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• 2000

• 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.

• Applied Biological Chemistry
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• v.29 no.1
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• pp.51-56
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• 1986

Using milled barley of four varieties Olbori, Youngsan-bori, Sacheon 6, and Suwon 228, the barley proteins were fractionated by the Osborne method and the modified Osborne method. Two fractionation methods were compared. There was a steady increase in the amount of nitrogen extracted as NaCl concentration increased, reaching a maximum at 0.5M NaCl and the extraction of nitrogen by 0.5M NaCl reached a maximum at $22^{\circ}C$. Alcohol-soluble fraction was least extracted by 70% (v/v) ethanol at $4^{\circ}C$ and most by sequential extraction with 50% (v/v) propan-1-ol alone followed by 50% (v/v) propan-1-ol plus 3% (v/v) 2-mercaptoethanol. Nitrogen was least extracted between pH 4 and 6 and most extracted at higher pH than 10. The modified Osborne fractionation of the protein complex in the four barleys showed that the salt-soluble nitrogen accounted for 21,4% to 24.1%, hordein-I varied from 30.4% to 43.4%, hordein-II varied widely from 9.3% to 19.5% and borate buffer-soluble glutelin content ranged from 17.1% to 23.7%.

• Proceedings of the Korean Society of Crop Science Conference
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• 2001.05a
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• pp.254-255
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• 2001

• Proceedings of the Korean Society of Crop Science Conference
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• 2001.05a
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• pp.256-257
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• 2001