• 한국작물학회지
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• 제49권2호
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• pp.141-147
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• 2004

This study was carried out to know the variation of soybean seed proteins, 11S and 7S globulins, and their amino acid compositions among different colored soybean varieties, 'Danbaegkong' (yellow), 'Pureunkong' (green) 'Jinyulkong' (brown), and 'Geoumjeongkong l' (black). Soybean seed proteins showed a wide range in molecular size, but the electrophoresis patterns of total seed protein subunits showed a similarity among different colored soybean varieties. Amino acid compositions of total seed proteins were similar for all soybean varieties tested. However, soybean varieties showed low composition rates in sulfur containing amino acids. The composition rates of cysteine and methionine in the 11S globulins were higher than those of total seed proteins and 7S globulins. Glutamic acid and glycine were higher in the 11S and 7S globulins than those of total seed proteins. However, the levels of methionine and phenylalanine are high in the 11S globulins, but those of valine and lysin are slightly lower than the 7S globulins. By using HPLC, we tried to analyse the soybean seed proteins. The 11S globulin was composed of 10 major peaks whereas the 7S globulin was composed of 4 major peaks. The composition rates of 11S related proteins have a tendency to increasing during the maturing whereas those of 7S related proteins have a tendency to decreasing. Composition rates of each peaks among different colored soybean varieties suggested that soybean seed proteins are varied, although they showed similarity in the electrophoresis patterns, and understanding of this characteristics is important for the utilization of soybeans.

• 한국지역사회생활과학회지
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• 제18권3호
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• pp.399-406
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• 2007

Soybean seeds were fermented by Bacillus subtilis and/or Lactobacillus bulgaricus to improve solubility, viscosity, water holding capacity and oil holding capacity of soybean proteins in Chongkukjang. The maximum colony forming unit and protease activity of B. subtilis or L bulgaricus were observed after 60 hours of fermentation, and those of the mixed fermentation by two microorganisms were steadily increased during the fermentation periods. Solubilities of soybean proteins by B. subtilis or L bulgaricus were steadily increased before the values were considerably increased to 60 hours of fermentation, whereas water holding capacities of the proteins were decreased by B. subtilis or L. bulgaricus and those of the mixed fermentation were decreased progressively. Viscosities of soybean proteins by B. subtilis and/or L. bulgaricus were decreased progressively during the fermentation. Viscosities of soybean proteins by B. subtilis and/or L. bulgaricus were decreased progressively during the fermentation. Oil holding capacities of soybeans by B. subtilis or L. bulgaricus were maximum at 20 or 80 hours of fermentation and those of the mixed fermentation were decreased after 10 hours of the fermentation.

• Journal of Plant Biotechnology
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• 제47권3호
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• pp.209-217
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• 2020

The presence of high amounts of seed storage proteins (SSPs) improves the overall quality of soybean seeds. However, these SSPs pose a major limitation due to their high abundance in soybean seeds. Although various technical advancements including mass-spectrometry and bioinformatics resources were reported, only limited information has been derived to date on soybean seeds at proteome level. Here, we applied a tandem mass tags (TMT)-based quantitative proteomic analysis to identify the significantly modulated proteins in the seeds of two soybean cultivars showing varying protein contents. This approach led to the identification of 5,678 proteins of which 13 and 1,133 proteins showed significant changes in Daewon (low-protein content cultivar) and Saedanbaek (high-protein content cultivar) respectively. Functional annotation revealed that proteins with increased abundance in Saedanbaek were mainly associated with the amino acid and protein metabolism involved in protein synthesis, folding, targeting, and degradation. Taken together, the results presented here provide a pipeline for soybean seed proteome analysis and contribute a better understanding of proteomic changes that may lead to alteration in the protein contents in soybean seeds.

• 한국작물학회지
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• 제59권3호
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• pp.359-363
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• 2014

Soybean seed is a good source of plant protein in human consumables such as baby formula and protein concentrate. The seeds contain an abundance of storage proteins, namely ${\beta}$-conglycin and glycinin that account for ~ 70-80% of the total seed protein content. Proteome profiling has been proved to be an efficient way that can help us to investigate the seed storage proteins. In the present study, the seeds were removed from the pods and the cotylendonary tissues were separated from the testa for proteome analysis in order to investigate the seed storage proteins. A systematic proteome profiling was conducted through one-dimensional gel electrophoresis followed by MALDI-TOF-TOF mass spectrometry in the seeds (cotyledonary tissue) of soybean genotypes. Two dimensional gels stained with CBB, a total of 10 proteins were identified and analyzed using MASCOT search engine according to the similarity of sequences with previously characterized proteins along with the UniProt database. A total of ten proteins such as glycinin Gy4 precursor, glycinin G3 precursor, glycinin G1 precursor, glycinin chain A2B1a precursor, glycinin chain A2B1a precursor were identified in our investigation. However, the glycinin subunit may be considered to play important roles in soybean breeding and biochemical characterization. In addition, the improved technique will be useful to dissect the genetic control of glycinin expression in soybean.

• The Plant Pathology Journal
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• 제23권4호
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• pp.281-286
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• 2007

Interactions between viral proteins and host proteins are essential for virus replication. Especially, translation of viral genes completely depends on the host machinery. In potyviruses, interactions of genome-linked viral protein (VPg) with host translation factors including eIF4E, eIF(iso)4E, and poly(A)-binding protein (PABP) has previously been characterized. In this study, we investigated interactions between Soybean mosaic virus (SMV) viral proteins and host translation factors by yeast two-hybrid system. SMV VPg interacted with eIF4E, eIF(iso)4E, and PABP in yeast two-hybrid system, while SMV helper component proteinase (HC-pro) interacted with neither of those proteins. The interaction between SMV NIb and PABP was also detected. These results are consistent with those reported previously in other potyviruses. Interestingly, we found reproducible and specific interactions between SMV coat protein (CP) and PABP. Deletion analysis showed that the region of CP comprising amino acids 116 to 206 and the region of PABP comprising amino acids 520 to 580 are involved in CP/PABP interactions. Soybean library screening with SMV NIb by yeast two-hybrid assay also identified several soybean proteins including chlorophyll a/b binding preprotein, photo-system I-N subunit, ribulose 1,5-biphosphate carboxylase, ST-LSI protein, translation initiation factor 1, TIR-NBS type R protein, RNA binding protein, ubiquitin, and LRR protein kinase. Altogether, these results suggest that potyviral replicase may comprise a multi-protein complex with PABP, CP, and other host factors.

• 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.

• 한국식품과학회지
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• 제22권7호
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• pp.805-811
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• 1990

대두단백질의 기능성을 개선하기 위하여 고정화된 트립신 및 키모트립신으로 가수분해시킨 후, 이 대두단백 가수물의 기능성을 조사하였다. Ferguson plot으로부터 가수분해물의 평균분자량 및 평균전하를 계산하여 대두단백의 기능성을 나타내는 인자로 이용하였다. 즉, 단백질의 평균분자량을 평균전하로 나눈 값은 단백가수물의 용해도, 포수력, 포유력, 유화도 등의 기능성을 예측하는데 이용될 수 있었다. 이 분자비가 낮으면 용해도는 향상되었으나 포수력은 감소되었으며 중간범위일 경우 포유력과 유화도는 증가되는 경향을 나타냈다.

• 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.

• 생명과학회지
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• 제5권2호
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• pp.57-62
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• 1995

Casein or soybean protein was subjected to there action with caffeic acidtyrosinase system at 30-35$\circ$C, pH 6.8 with aeration for 5hr. The resulting brown proteins were washed with acetone until the washings were on longer colored. However, modified protein still retained a light brown. The effects of the modified proteins and brown compounds on male Wistar strain rats were studied by pair-feeding of a cholesterol-free diet for 14days. Significant decrease in protein digestibility for the rats fed with the modified proteins were observed. Weight gain and protein digestibility were not influenced by feeding brown compounds, but the feeding of brown compound from casein caused an enlargement of caecum. The concentrations of serum cholesterol and triglyceride in the rats fed with modified proteins and brown compounds were mostly unchanged against the rats fed with untreated proteins. These results suggest that the decrease in protein digestibility induced by enzymic browning-reaction did not cause the decrease in concentration of serum cholesterol.

• Journal of Plant Biotechnology
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• 제47권2호
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• pp.118-123
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• 2020

The black seed coat of soybeans contain anthocyanins which promote health. However, mature soybean seeds contain anti-nutritional factors like lipoxygenase, lectin and Kunitz Trypsin Inhibitor (KTI) proteins. Furthermore, these seeds can be used only after the genetic elimination of these proteins. Therefore, the objective of this study was to develop novel soybean genotypes with black seed coat and triple recessive alleles (lx1lx1lx2lx2lx3lx3, titilele) for lipoxygenase, lectin, and KTI proteins. From a cross of parent1 (lx1lx2lx3/lx1lx2lx3, ti/ti, Le/Le) and parent2 (lx1lx2lx3/lx1lx2lx3, Ti/Ti, le/le), 132 F₂ seeds were obtained. A 3:1 segregation ratio was observed during F₂ seed generation for the inheritance of lectin and KTI proteins. Between a cross of the Le and Ti genes, the observed independent inheritance ratio in the F₂ seed generation was 9: 3 : 3 : 1 (69 Le_Ti_: 32 leleTi_: 22 Le_titi: 9 leletiti) (χ²=2.87, P=0.5 - 0.1). From nine F₂ seeds with triple recessive alleles (lx1lx1lx2lx2lx3lx3, titilele genotype), one novel strain posessing black seed coat, and free of lipoxygenase, lectin and KTI proteins, was selected. The seed coat color of the new strain was black and the cotyledon color of the mature seed was green. The weight of 100 seeds belonging to the new strain was 35.4 g. This black soybean strain with lx1lx1lx2lx2lx3lx3, titilele genotype is a novel strain free of lipoxygenase, lectin, and KTI proteins.