• 제목/요약/키워드: seed storage protein

검색결과 103건 처리시간 0.019초

Characterization of 7S and 11S Globulins in Soybean Varieties Differing in Seed Size and Their Effects on the Properties of Soybean Curd

  • Kim, Sun-Lim;Koo, Han-Mo;Chun, Se-Cheol;Kim, Jung-Tae;Kim, Min-Young;Chi, Hee-Youn;Kim, Eun-Hye;Kim, Hyun-Bok;Kim, Mi-Jung;Seo, Bo-Ram;Kang, Eun-Young;Seo, Su-Hyun;Chung, Ill-Min
    • Food Science and Biotechnology
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    • 제17권1호
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    • pp.135-143
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    • 2008
  • The ratio between 11S Sand 7S globulins was greater in large seed size varieties (LSSVs) of soybean than in small seed size varieties (SSSVs) or medium seed size varieties (MSSVs) but did not differ between MSSVs and SSSVs. The cysteine and methionine contents of 11S globulins were greater than those of total seed proteins and 7S globulins. The acidic monoamino monocarboxylic amino acids were the most abundant class of amino acid in soybean seed (27.2%) and soybean curd protein (29.3%). Isolated 7S and 11S fractions were analyzed by HPLC. Of the 12 peaks detected, 4 constituted 64.1% of the proteins of the SSSVs, 65.6% of the proteins of the MSSVs, and 70.5% of the proteins of the LSSVs. The 11S/7S globulin ratio was related to the yield and hardness of soybean curd. The MSSVs had the greatest yield of soybean curd, but the soybean curd hardness of the MSSVs was greater than that of the SSSVs. These results show that the 11S/7S ratio and color of soybean seeds can be used to predict the yield, hardness, and color of soybean curd.

$\beta$-Conglycinin의 대장균 발현과 정제 (Expression and purification of Soybean $\beta$-Conglycinin from)

  • 노영희
    • 한국식품영양학회지
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    • 제12권2호
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    • pp.184-190
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    • 1999
  • Soybean protein consists of two major components $\beta$-conglycinin and glycinin which together consti-tute 70% of the total seed storage protein at maturity. $\beta$-Conglycinin is trimeric glycoprotein and for-med by the assembly of various combinations of three subunits $\alpha$,$\alpha$' and $\beta$ which have molecular weig-hts of 69,000, 72,000 and 42,000, respectively. Recently $\beta$-conglycinin was identified as powerful LDL lip-oprotein receptor activation hypercholesterolemia and major allergenic proteins. To investigate these reasons we constructed an expression system of cDNA encoding $\alpha$-subunit of $\beta$-conglycinin in Escherichia coli and purified the expressed protein. The pro-$\beta$-conglycinin synthesized in Escherichia coli BL 21 (DE3)comprised approximately 15% of the total bacterial proteins and the expressed protein are formed sol-uble and trimer such as native protein in Escherichia coli cells. The highly expressed protein was purified to homogeneity by salt precipitation with 20~40 % ammonium sulfate ion-exchange chromatography with Q-sepharose and hydrophobic column chromatography with Butyltoyopearl.

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A Simple and Rapid Method to Isolate Low Molecular Weight Proteinase Inhibitors from Soybean

  • Krishnan Bari B.
    • 한국작물학회지
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    • 제49권4호
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    • pp.342-348
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    • 2004
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the $60\%$ isopropanol extract of soybean(Glycine max [L.] Merr.) seed revealed two abundant proteins with molecular masses of 19 and 10 kDa. Amino acid analysis revealed that the isopropanol-extractable protein fraction was rich in cysteine. Two-dimensional gel electro-phoretic analysis indicated that the 19kDa and 10kDa proteins had pI of 4.2 and 4.0 respectively. Peptide mass fingerprints of trypsin digests of the two proteins obtained using matrix-assisted, laser desorption/ionization-time of flight (MALDI-TOF) mass spectroscopy revealed the 19kDa protein was Kunitz trypsin inhibitor and the 10kDa protein was Bowman-Birk proteinase inhibitor. When resolved under non-denaturing conditions, the isopropanol-extracted proteins inhibited trypsin and chymotrypsin activity. Results presented in this study demonstrate that isopropanol extraction of soybean seed could be used as a simple and rapid method to obtain a protein fraction enriched in Kunitz trypsin and Bowman-Birk proteinase inhibitors. Since proteinase inhibitors are rich in sulfur amino acids and are putative anticarcinogens, this rapid and inexpensive isolation procedure could facilitate efforts in nutrition and cancer research.

자포니카 및 통일형 벼 품종에서의 식미 관련 저장단백질 특성 (Characteristics of Seed Storage Protein Affecting the Eating Quality of Japonica and Tongil-type Rice)

  • 곽지은;이점식;윤미라;김미정;천아름;이춘기
    • 한국작물학회지
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    • 제61권4호
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    • pp.227-234
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    • 2016
  • 본 연구에서는 쌀의 저장 단백질 조성 분석을 통해 자포니카와 통일형 품종의 식미 특성 차이를 구명하고자 하였다. 쌀의 저장단백질 분석 결과, 통일형 품종은 자포니카 품종에 비해 알부민과 글로부린이 각 1.2배, 1.3배, 글루텔린의 서브유닛인 산성 글루텔린 ${\alpha}-2$의 비율이 약 1.3배 낮은 반면, 글루텔린의 서브유닛인 산성 글루텔린 ${\alpha}-1$ 비율은 1.7배 높은 특성을 나타냈다. 또한, 저장단백질 조성과 식미특성의 상관성 분석을 실시한 결과, 식미 총평은 알부민(R=0.495, p<0.01), 글로부린(R=0.567, p<0.01)과 정의상관을 보였으며 산성 글루텔린 유닛인 ${\alpha}-1$은 총평과 뚜렷한 부의 상관(R=-0.612, p<0.01)이 인정되었다. 식미 총평 이외에도 밥의 외관, 맛, 찰기, 질감과 관련하여 알부민은 정의 상관, ${\alpha}-1$ 글루텔린은 부의 상관관계를 나타냈다. 생태형에 따른 저장단백질 비율이 식미 특성에 미치는 영향을 구명하기 위해 저장단백질 비율과 식미 특성과의 상관 분석을 실시한 결과, 산성 글루텔린의 서브유닛인 ${\alpha}-1$, 알부민, 글로부린이 통일형 품종의 식미 특성에 영향을 주는 것으로 보이며 향후, 다양한 품종을 이용한 추가 연구를 통해 정밀한 해석이 필요할 것으로 생각된다.

발아중 빛에 의한 무 유식물의 자엽 Microbody의 활성 변화 (Effect of Light on Developmental Changes and Activities of Microbody in the Cotyledons of Radish Seedlings)

  • 박민철
    • Journal of Plant Biology
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    • 제29권4호
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    • pp.243-254
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    • 1986
  • The enzyme patterns and the food storage changes in radish (Raphanus sativus L. cv. Taewang) cotyledons during seedling development were studied. The radish seeds were germinated for 8 days at $25^{\circ}C$ under light (7, 000 lux) or dark condition. The lipid and protein contents per seed were 4.3 mg and 2.85 mg respectively. In 8-day-old light-grown seedling, the lipid and protein contents per cotyledon pair were 1.5 mg and 2.08 mg; in 8-day-old dark-grown seedling, they were 0.8 mg and 1.24 mg respectively. The heterotrophic phase of seedlings continued for 3 days after sowing and followed by autotrophic phase (3~6 day) and senescence phase (6~8 day). The food storage function decreased in response to time course. During heterotrophic phase, the activities of glyoxysomal enzymes (malate synthetase, isocitrate lyase, and catalase) were high at 2~3 day. Those patterns were somewhat more prominent in darkness. During the autotrophic phase, the activities of peroxysomal enzymes (glycolate oxidase and catalase) increased at 4~5 day.

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The Use of Lupins in Feeding Systems - Review -

  • Petterson, D.S.
    • Asian-Australasian Journal of Animal Sciences
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    • 제13권6호
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    • pp.861-882
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    • 2000
  • The seed, or grain, of modern cultivars of Lupinus angustifolius, commonly known as Australian sweet lupins (ASL), is an established feed resource for the intensive animal industries of Australia, Japan, Korea and several other countries in Asia and Europe. Since the introduction of ASL to the world marketplace about 25 years ago, researchers in many countries have found them to be a valuable component of the diet of beef and dairy cattle, sheep, pigs, poultry, finfish and crustaceans. The seed of ASL contains ~32% crude protein (CP) (~35% DM basis) and 5% oil. The main storage carbohydrates in the seed are the ${\beta}$-galactans that comprise most of the cell-wall material of the kernel and the cellulose and hemicellulose of the thick seed coats. ASL seeds contain about 40% non-starch polysaccharides (NSP) and a negligible amount of starch. This makes them an excellent ingredient for ruminant diets, as the risk of acidosis is very low. The seed of modern cultivars of domesticated Lupinus species contain negligible amounts of lectins and trypsin inhibitors so they do not require preheating before being used as an ingredient in feeds for monogastric species. They have a high digestibility coefficient for protein, >90% for most species, but a low energy digestibility, ~60%, which is mostly due to the high content of NSP. The low content of methionine (0.22%) and of lysine (1.46%) is typical of the legumes. The lysine availability for pigs is >70%. Lupin kernels contain ~39% CP (~42% DM basis), 6% oil and 30% NSP. They have a higher digestible energy for pigs and finfish and a higher metabolisable energy for poultry than whole seed. Commercial operations rarely achieve complete separation of kernel from hull and it is more likely that the kernel fraction, called splits or meats, will contain ~36% CP. The replacement of soybean meal or peas with ASL in cereal-based diets for most intensively reared animals, birds and fish is possible provided lysine, methionine and digestible energy levels are kept constant. This makes ASL economically competitive in many, but not all, circumstances.

콩 종실 단백질의 유전변이 (Genetic variation of 7S and 11S globulins in soybean seed)

    • 한국자원식물학회지
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    • 제12권3호
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    • pp.198-203
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    • 1999
  • 콩 저장 단백질의 대부분은 globulin이며, 이중 7S와 11S가 70% 이상을 차지한다. 따라서 콩 단백질의 조성개량을 위해서는 11S/7S비율 조정이 우선되는데, 본 연구에서는 전기영동(SDS-PAGE)법을 사용하여 콩 단백질 7S와 11S를 분리 확인하고, 이들 분획 단백질의 유전변이를 분석하였다. 국내 3개지역에서 재배된 콩 장려품종 6계통들의 평균 7S 함량은 38.9% 이었고 11S는 61.2%의 함량을 나타내었다. 분산분석 결과 품종간에 는 유의성이 있었지만 지역간에는 변이가 없었으며, 품종 x 지역의 상호작용은 고도의 유의성을 나타내었다. 유전력은 7S분획중의 $\beta$함량이 72.7%로 높게 나타났다. 공분산을 이용한 상관계수 추정에서는 유전상관이 표현형 상관 보다 다소 높게 나타났다. 따라서 7S와 11S의 분획간 함량을 조정함으로써 콩 단백질의 조성을 개량할 수 있으리라 판단된다.

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벼 종자 저장단백질 및 재설계 연구 동향 (New design of rice seed storage proteins)

  • 김영미;이종렬;윤웅한;최상봉;하선화;임선형
    • Journal of Plant Biotechnology
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    • 제38권4호
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    • pp.263-271
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    • 2011
  • 벼는 세계 인구의 60%에 의해 소비되고 있는 주요 식량작물이며 그 종자의 주성분은 탄수화물로 인류의 중요한 에너지원이 된다. 미곡(米穀)은 주식으로 다량 섭취하게 되는데 특히 동물성 단백질의 섭취가 부족한 국가 또는 지역에서는 쌀 단백질이 콩 단백질과 함께 중요한 영양공급원이 되고 있어 벼의 종자단백질은 인류에 매우 중요한 영양성분이라 할 수 있다. 그런데 벼의 종자단백질은 필수아미노산인 라이신이 부족하므로 아미노산 조성 변경에 의한 영양적인 개량이 요구되기도 하는 한편 선진국에서는 혈압조절이나 면역증강 등 생리기능을 가진 건강증진용 기능성 단백질 또는 펩티드로 주목받고 있다. 따라서 벼의 종자단백질의 조성변경과 더불어 이종의 저장단백질의 도입에 의한 벼 종자단백질 개량 연구가 진행되어 왔다. 본 총설에서는 벼의 종자 저장단백질의 생합성과 축적 특징 및 저장단백질 집적의 유전적 제어 기작에 대하여 알아보고 또한 벼 종자 저장단백질 조성 변경, 이종단백질 도입에 의한 벼 종자 저장단백질 개량 연구 현황을 기술하고자 한다.

Changing Wheat Quality with the Modification of Storage Protein Structure

  • Tamas, Laszlo;Bekes, Ferenc;Morrell, Matthew K.;Appels, Rudi
    • Journal of Plant Biotechnology
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    • 제1권1호
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    • pp.13-19
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    • 1999
  • The visco-elastic properties of gluten are major determinants of the processing properties of doughs. These visco-elastic properties are strongly influenced by the ratio of monomeric and polymeric proteins and the size distribution of the polymeric proteins, which make up the gluten fraction of the dough. Recent studies have revealed that other features, such as the number of the cysteine residues of the HMW-GS, also play an important role in determining the functional characteristics. To modify the processing properties at molecular level, the relationship between the structure of molecules and dough properties has to be understood. In order to explore the relationships between individual proteins and dough properties, we have developed procedures for incorporating bacterially expressed proteins into doughs, and measuring their functional properties in small-scale equipment. A major problem in investigating the structure/function relationships of individual seed storage proteins is to obtain sufficient amounts of pure polypeptides from the complex families of proteins expressed in the endosperm. Therefore, we have established a simplified model system in which we produce specific protein genes through bacterial expression and test their functional properties in smallscale apparatus after incorporation into base flour. An S poor protein gene has been chosen as a template gene. This template gene has been modified using standard recombinant DNA techniques in order to test the effects of varying the number and position of cysteine residues, and the size of the protein. Doughs have been mixed in small scale apparatus and characterized with respect to their polymeric composition and their functional properties, including dough mixing, extensibility and small scale bating. We conclude that dough characteristics can be manipulated in a predictable manner by altering the cysteine residues and the size of high molecular weight glutenins.

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콩의 7S α' - subunit 단백질의 유전 (Inheritance of 7S α' - subunit Protein in Soybean Seed)

  • 성미경;김경록;박정수;황교진;정종일
    • 농업생명과학연구
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    • 제43권5호
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    • pp.39-42
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    • 2009
  • 인간과 가축의 영양을 위한 식물성 단백질의 주요 공급원은 콩이며 콩 단백질은 영양 및 기능성면에서 우수하여 소비가 점차 증가하고 있다. 그러나 콩 단백질에는 알러지를 일으키고 영양가치를 떨어뜨리는 성분도 포함되어져 있다. 7S 및 11S 글로블린은 콩 저장단백질의 대부분을 차지하며 7S는 영양가치가 떨어지고 7S의 함량을 줄어든 콩 계통 육성에 대한 관심이 높아지고 있다. 7S 성분중의 하나인 ${\alpha}^{\prime}$-subunit의 유전양상을 파악하기 위하여 진품콩2호와 PI506876의 교배로부터 98개의 F2 종자가 얻어졌다. SDS-PAGE로 각각의 종자를 분석한 결과 ${\alpha}^{\prime}$-subunit을 가진 종자가 70개였고 결핍된 종자가 28개였다. 이러한 유전양상은 단인자 유전원칙 (${\chi}^2=0.667$, P=0.414)과 일치하여 콩 종자에서 7S의 ${\alpha}^{\prime}$-subunit 단백질은 한 개의 유전자에 의 해서 좌우되었다. 이 결과는 7S 단백질 함량이 줄어든 콩 계통 선발에 유용하게 활용될 것으로 기대된다.