• Title/Summary/Keyword: glutenin

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Studies on the Chemical Composition of Korean Wheat Flour Proteins (I). Purification of Gliadin Proteins and Amino Acid Composition (한국산 밀가루 단백질의 화학적 조성에 관한 연구 (제1보). Gliadin 단백질의 아미노산 조성 및 그의 정제)

  • Sung Hye Cho;Kim Jun Pyong
    • Journal of the Korean Chemical Society
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    • v.21 no.3
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    • pp.210-214
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    • 1977
  • We have investigated the amino acid composition of gliadin and glutenin from wheat flour Jang Kwang variety and have purified the main gliadin protein by Sephadex column. The results were obtained as follows: 1. Five bands of component for both gliadin and glutenin were found in disc electrophoretic gel column 2. The highest content of amino acid in gliadin and glutenin were glutamic acid and alanine was present in comparatively large amounts in glutenin, whereas proline was rich in gliadin 3. Main gliadin protein was purified by Sephadex G-150 and A-25 column chromatography and identified its purity by disc electrophoresis.

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밀가루 단백질의 화학적 구성

  • 김준평
    • Food Industry
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    • s.19
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    • pp.15-19
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    • 1974
  • 밀가루 단백질인 Gluten은 밀가루 반죽의 부피를 크게하는 중요한 역할을 하며 이 Gluten 단백질을 구성한 Gliadin의 분자량은 40,000이며 Glutenin은 2$\~$3백만의 고분자화합물로 Gliadin과 Glutenin은 서로 구조상으로는 다르나 Gliadin이 Glutenin 구성 polypeptide로 S-S 결합에 중합체로 구성하며 이들은 20,000$\~$25,000정도의 공통된 polypeptide로부터 이루어진 것으로 추리하고 있다. Gluten 단백질에 S-S 함량이 7.4$\~$10mole/$10^5$g protein이며 -SH 함량은 0$\~$0.3mole/$10^5$g protein이다. Gluten 표면에 -SH가 적으나 S-S, 및 -SH의 상호교환이 일어나 망상 형성하여 밀가루 반죽내에서 발생하는 $CO_2$의 가스를 들어쌓여 빵의 부피를 크게 한 것이다.

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Allelic Variation of Glutenin, Granule-Bound Starch Synthase l and Puroindoline in Korean Wheat Cultivar

  • Park, Chul-Soo;Pena, Roberto J.;Baik, Byung-Kee;Kang, Chon-Sik;Heo, Hwa-Young;Cheong, Young-Keun;Woo, Sun-Hee
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.54 no.2
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    • pp.181-191
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    • 2009
  • To investigate the genetic variation of high-and low-molecular-weight glutenin subunits (BMW-GS and LMW-GS), granule-bound starch synthase I (GBSSI) and puroindoline in 24 Korean wheat cultivars. At the BMW-GS compositions, three Glu-A1 alleles, five Glu-B1 alleles and three Glu-D1 alleles were identified. The high frequency of alleles at each locus was Glu-A1c allele (15 cultivars), Glu-B1b allele (16 cultivars) and Glu-D1f allele (16 cultivars). Four alleles were identified at the Glu-A3 and Glu-B3 loci and three at Glu-D3 locus and Glu-A3d, Glu-B3d and Glu-D3a were mainly found at each Glu-3 locus. Glu-A3d, Glu-B3d, Glu-D3b or c (4 cultivars, respectively) and Glu-A3d, Glu-B3d, Glu-D3a and Glu-A3c, Glu-B3d or h, Glu-D3a (3 cultivar, respectively) were predominantly found in Korean wheats. At the GBSS compositions, 2 waxy wheat cultivars, Shinmichal and Shinmichal1, showed null alleles on the Wx loci and other cultivars were wild type in GBSS compositions. At the puroindoline gene compositions, Korean wheat cultivars carried 3 genotypes, which 10 cultivars (41.7%) were Pina-D1a and Pinb-D1a, 11 cultivars (45.8%) had Pina-D1a and Pinb-D1b and 3 cultivars (12.5%) carried Pina-D1b and Pinb-D1a. These genetic variations could present the information to improve flour and end-use quality in Korean wheat breeding programs.

High Molecular Weight Glutenin Subunit in Common Wheat (Triticum aestivum L.) (밀의 고분자 글루테닌 단백질)

  • Lee, Jong-Yeol;Kim, Yeong-Tae;Kang, Chon-Sik;Lim, Sun-Hyung;Ha, Sun-Hwa;Ahn, Sang-Nag;Kim, Young-Mi
    • Korean Journal of Breeding Science
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    • v.43 no.5
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    • pp.479-489
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    • 2011
  • Gluten is the main functional component of wheat, and is the main source of the viscoelastic properties in a dough. One of the gluten group is glutenin, which is composed of high molecular weight (HMW) and low molecular weight (LMW) subunits. The HMW glutenin subunits (HMW-GS) have been shown to play a crucial role in determining the processing properties of the grain. They are encoded by the Glu-1 loci located on the long arms of homeologous group one chromosomes, with each locus comprising two genes encoding x- and y-type subunits. The presence of certain HMW subunits is positively correlated with good bread-making quality. The highly conserved N- and C- terminal contaning cystein residues which form interand intra-chain disulphide bonds. This inter chain disulphide bonds stabilize the glutenin polymers. In contrast, the repetitive domains that comprise the central part of the HMW-GS are responsible for the elastic properties due to extensive arrays of interchain hydrogen bonds. In this review, we discuss HMW-GS, HMW-GS structure and gluten elasticity, relationship between HMW-GS and bread wheat quality and genetic engineering of the HMW-GS.

Genetic Variation of High Molecular Weight Glutenin (HMW-Glu) Subunit in Korean Wheat

  • Hong, Byung-Hee;Park, Chul-Soo
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.43 no.4
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    • pp.259-263
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    • 1998
  • High molecular weight glutenin (HMW-Glu) subunit compositions of 73 Korean wheat cultivars and experimental lines were evaluated by using one dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This method is suitable for obtaining a good resolution of 1Dx2 and 1Ax2$^*$ without adverse effects on separation of other HMW-Glu subunits. Korean wheats examined in this study could be divided into 15 different groups on the basis of HMW-Glu subunit compositions. From the wheat lines tested, it was identified that there were three alleles at the Glu-Al, five at the Glu-Bl and three at the Glu-D1 loci. The null allele of the Glu-Al was occurred in high frequency (79.4%), while low frequencies for 1Ax1 (12.3%) and 1Ax2$^*$(8.2%) were found. High frequency (75.3%) of the subunit pairs of 1Bx7+1By8 at the Glu-Bl loci compared with other subunits was found. The frequencies of subunits 1Dx2. 2+1Dy12 and 1Dx2+1Dy12 from the Glu-D1 loci were 54. 8% and 37.0%, respectively. However, a few Korean wheat lines (8.2%) carried 1Dx5 + 1Dy10 subunit pair which are responsible for good breadmaking quality. The information of HMW-Glu subunit compositions provide a useful tool to characterize wheat lines, and can be directly used in selection of breeding lines of different end-use properties.

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Flour Characteristics and End-Use Quality of Korean Wheats with 1Dx2.2+1Dy12 Subunits in High Molecular Weight Glutenin

  • Park, Chul-Soo;Baik, Byung-Kee;Kang, Moon-Seok;Park, Jong-Chul;Park, Jae-Gun;Yu, Chang-Yeon;Choung, Myoung-Gun;Lim, Jung-Dae
    • Preventive Nutrition and Food Science
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    • v.11 no.3
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    • pp.243-252
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    • 2006
  • White salted noodles and pan bread were prepared from Korean wheats with 1Dx2.2+1Dy12 subunits in high molecular weight glutenin subunits (HMW-GS) to evaluate the suitability for end-use products through the comparison with US wheats with various classes and commercial wheat flours. Korean wheat flours with 1Dx2.2+1Dy12 subunits showed higher SDS sedimentation volume than US wheat flours with similar protein content. Compared to wheat flours with similar protein content and SDS sedimentation volume, water absorption percent of Korean wheat flours using a mixograph was higher than that of US wheat flours, but similar to commercial wheat flours. Mixograph mixing time was similar to hard wheat flours and commercial noodle flours. Optimum water absorption percent of noodle dough from Korean wheat flours was higher than that of US wheat flours. Noodle sheets from Korean wheat flours with 1Dx2.2+ 1Dy12 subunits showed lower L values, higher a values and similar b values compared to commercial noodle flours. Hardness of cooked noodles from Korean wheat flours 1Dx2.2+1Dy12 subunits correlated positively with protein content, NIRS hardness, mixograph water absorption and gluten yield of flours. Korean wheat flours with 1Dx2.2+1Dy12 subunits showed lower loaf volume and harder crumb firmness than hard wheat flours and commercial bread wheat flours in spite of similar protein quantity and quality to hard wheat flours.

Comparison of Allergy-Inducible Wheat Protein Contents among Imported and Domestic Wheat Flours in Korea

  • Kim, Ju Hee;Pak, Pyo June;Kim, Jung-Gon;Cheong, Young-Keun;Kang, Chon-Sik;Lee, Nam Taek;Chung, Namhyun
    • Journal of Applied Biological Chemistry
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    • v.59 no.1
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    • pp.1-3
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    • 2016
  • Wheat is a staple food in the Korean diet, which is increasingly becoming westernized. Because most domestic wheat consumption relies on imported wheat, we aimed to evaluate the allergy-inducible protein contents of commercial flours from imported and domestic wheat. Analysis of the protein contents by densitometry suggested that domestic wheat flours contain lower levels of high molecular weight glutenin and omega-gliadin (50 and 34% lower, respectively) than imported wheat flours. Therefore, domestic wheat flours are less likely to cause allergic reactions than imported wheat flours are. Based on the findings of our study, were commend increased consumption of domestic wheat flours to those who are sensitive to allergy.

A Comparison of Protein Characteristics of Korean and Imported Wheat Varieties (한국산 소맥과 수입 소맥의 단백질 특성 비교)

  • Koh, Bong-Kyung
    • Korean Journal of Food Science and Technology
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    • v.31 no.3
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    • pp.586-592
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    • 1999
  • The objective of this study was to investigate the fundamental characteristics of proteins effecting on Korean wheat flour quality. Mixing properties and protein contents of Eunpa, Allgreu, and Woori showed soft wheat characteristics. Tapdong had strong dough stability and high protein content like hard wheat flour. However, even though Greu had a high protein content, the dough strength was very weak like soft wheat flour. No major difference was observed in protein solubility with water, 0.1N NaCl, 70% ethyl alcohol, 0.1 N acetic acid solution and in sulfur and disulfide contents between Korean wheat flours and imported flours. However, DNS (Dark Norther Spring) had more contents of acid insoluble and SDS insoluble proteins compared with Korean wheat varieties. PAGE pattern of Tapdong was very similar to imported wheat flours at the high molecular weight regions and characteristic high molecular weight glutenin subunits were observed over 116 kD protein molecular weight region from 4 Korean wheat flours such as Eunpa, Woori, Allgreu, and Greu.

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