• 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.

• Proceedings of the Korean Society of Crop Science Conference
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• 2022.10a
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• pp.18-18
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• 2022

Barley has been used for the production of malt in the brewing industry. Malting is the process of preparing barley through partial germination. Malt extract is the most important quality parameter for malt quality. The grain and malt quality parameters of ten Korean malting barley varieties were studied. Malts was prepared using Phoeix automated micro malting system(Phoenix Bio, Australia). Quality analysis of Barley and malt was determined according to European brewery convention(EBC, 1998) and American society of brewing chemists(ASBC, 1997) method. And the hordeins of barley and malt were extracted with 50% isopropyl alcohol(IPA, 2-propanol) of 1% dithiothreitol(DTT). The analysis of hordeins was carried out by ultra-performance liquid chromatography(UPLC). The mean values of 1000-grains weight, assortment rate, protein content, starch content, beta-glucan content, husk rate, germination energy, germination capacity and water sensitivity of grain were 45.8g, 86.8%, 11.9%, 58.0%, 3.8%, 14.0%, 96.2%, 97.2%, 10.0%, respectively. The mean values of protein content, friability, diastatic power, extract, soluble protein, Kolbach index, beta-glucan of malt and wort were 11.3%, 87.6%, 201WK(Windish Kolbach), 79.3%, 4.6%, 41%, 85mg/L, respectively. UPLC analysis of grain and malt hordeins revealed that the amount of hordeins significantly degraded during malting. Also, we could successfully be used to compare hordein polypeptide patterns with malt quality.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.57 no.2
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• pp.171-181
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• 2012

Lysine is the first limiting essential amino acid in cereals for humans and monogastric animals, although its content is generally low. A chemically induced high-lysine barley mutant, M98, has an agronomically undesirable shrunken endosperm trait. In order to obtain detailed insight into the atypical traits of M98 grains, we characterized amino acid composition and protein profiles of M98 and its parent cultivar Chalssalbori. Among a total of 16 amino acids, the percentage of each of the 7 amino acids, including lysine, was 1.2~1.8 times higher in M98, comparing to Chalssalbori. The percentage of proline and its precursor, glutamic acid, in M98 was about the half of that of the amino acids in Chalssalbori, but arginine synthesized from glutamic acid was 1.8 times higher in M98, compared that in the parent cultivar. Theses results indicated that the mutation in M98 grains might alter the proportion of amino acids linked to each other in a biosynthetic pathway. A comparison of grain proteome profiles between Chalssalbori and M98 revealed 70 differentially expressed protein spots, where 45 protein spots were up-regulated and 25 protein spots down-regulated in M98 compared to those in Chalssalbori. Of these changed protein spots, 53 were identified using nano-electrospray ionization liquid chromatography mass spectrometry. Most of these identified proteins were involved in various biological processes. In particular, 28 protein spots such as ${\beta}$-amylase, serpins and B3-hordein were identified as proteins associated with the atypical traits of M98. It was thought that a genetic study on the unique protein profile of M98 would be needed to develop an agronomically feasible barley cultivar with high-lysine trait.