• Journal of Plant Biotechnology
• /
• v.47 no.2
• /
• pp.118-123
• /
• 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.

• Journal of Microbiology and Biotechnology
• /
• v.10 no.2
• /
• pp.251-257
• /
• 2000

Chitin synthases are identified as key enzymes of chitin biosynthesis in most of the fungi. Among them, chitin synthase II has been reported to be and essential enzyme in chitin biosynthesis, and exists as a membrane-bound form. To search and screen new antifungal agents from natural resources to inhibit chitin synthase II, the assay conditions were established using the enzyme isolated from Saccharomyces cerevisiae ECY38-38A(pAS6) that overproduces only chitin synthase II. This enzyme was activated only by partial proteolysis with trypsin. Its actibity reached the maximum at $80{\;}\mu\textrm{g}/ml$ of trypsin and was strongly stimulated by 2.0 mM $Co^{2+}$, 1.0 nM UDP-[$^{14}C$]-GicNAc, and 32 mM free-GlcNAc. Under these assay conditions, the highest chitin synthase II activity was observed by incubation at $30^{\circ}C$ for 90 min. However, and extremely narrow range of organic solvents up to as much as 25% of DMSO and 25% of MeOH was useful for determining optimal assay conditions. After a search or potent inhibitors of chitin synthase II from natural resources, prodigiosin was isolated from Serratia marcescens and purified by solvent extration and silica gel column chromatographies. The structure of prodigiosin was determined by UV, IR, Mass spectral, and NMR spectral analyses. Its molecular weight and formula were found to be 323 and $C_{20}H_{25}N_{3}O$, respectively. Prodigiosin ingibited chitin synthase II by 50% at the concentration of $115{\;}\mu\textrm{g}/ml$.

• Applied Biological Chemistry
• /
• v.35 no.4
• /
• pp.232-236
• /
• 1992

In order to manufacture of soy paste, Changes of chemical composition and enzyme activity of soybean by different processing method were investigated. The results are summarized as follows: Changes of chemical compositions were; Raw(A) and soaked(B) soybeans contain about 2% of more crude fat than roasted(C) and steamed(D) soybeans, roasted and steamed soybeans contain $1.16{\sim}1.74%$ of more protein than those of raw and soaked soybeans, and Raw and roasted soybeans contain $0.11{\sim}0.41%$ of more crude fiber than those of soaked and steamed soybeans. ${\alpha}-amylase$, ${\beta}-amylase$, protease, lipase activity of raw and soaked soybeans were $2{\sim}5$ folds higher than those of roasted and steamed soybeans. Trypsin inhibitor activity of raw, soaked, roasted and steamed soybeans was indicated 56.7%, 42.9%, 32.9% and 20.8% in the order, respectively.

• The Plant Pathology Journal
• /
• v.28 no.2
• /
• pp.197-201
• /
• 2012

Potyviruses express their RNA genomes through the production of polyproteins that are processed in host cells by three virus-encoded proteases. Soybean plants produce large amounts of protease inhibitors during seed development and in response to wounding that could affect the activities of these proteases. The in vitro activities of two of the proteases of Soybean mosaic virus (SMV) and Tobacco vein mottling virus (TVMV) were compared in the rabbit reticulocyte lysate in vitro translation system using synthetic RNA transcripts. Transcripts produced from SMV and TVMV cDNAs that included the P1 and helper component-protease (HC-Pro) coding regions directed synthesis of protein products that were only partially processed. Unprocessed poly-proteins were not detected from transcripts that included all of the P1, HC-Pro, P3 and portions of the cylindrical inclusion protein coding regions of either virus. Addition of soybean trypsin inhibitor to in vitro translation reactions increased the accumulation of the unprocessed polyprotein from TVMV transcripts, but did not alter the patterns of proteins produced from SMV. These experiments suggest that SMV-and TVMV-encoded proteases are differentially sensitive to protease inhibitors.

• Korean Journal of Food Science and Technology
• /
• v.30 no.4
• /
• pp.751-758
• /
• 1998

Lipoxygenase-deficient soybeans, Jinpumkong (lipoxygenase-2, 3 lacking) and Jinpumkong 2 (lipoxygenase-1, 2, 3 lacking), were breeded for the improvement of beany flavor problem. The objectives of this study were to characterize and to examine the storage stability of two lipoxygenase-deficient soybeans by comparing with Hwangkeumkong having high lipoxygenase activity. The crude protein and crude lipid content of Jinpumkong 2 were lower than those of Hwkangkeumkong and Jimpumkong. All soybean samples were middle-sized and yellow-coated seeds. The rate of water uptake and trypsin inhibitor activity of Jinpumkong were greater than those of others. The cooking rate of Hwangkeumkong was the highest among all. The lipoxygenase activity of Hwangkeumkong was decreased when the soybeans were stored at $40^{\circ}C$ for 96hrs at 90% RH which is the condition of accelerated aging. After accelerated aging, the germination ratio of Hwangkeumkong was not changed but the ratio and speed of germination dropped rapidly in Jinpumkong and Jinpumkong 2.

• Korean Journal of Breeding Science
• /
• v.42 no.1
• /
• pp.35-39
• /
• 2010

Soybean proteins are widely used for human and animal feed in the world. ${\beta}$-conglycinin protein exhibits poor nutritional and food processing properties and Kunitz trypsin inhibitor (KTI) protein is a main anti-nutritional factor in soybean seed. The objective of this research was to identify the inheritance of $cgy_1$ gene and ti gene for the improvement of soybean cultivar with no KTI proteins and low amount of ${\beta}$-conglycinin. $F_2$ population was made by crossing between "Gaechuck2ho" (${\alpha}^{\prime}$-subunit present $Cgy_1Cgy_1$, KTI protein absent titi) and PI506876 (${\alpha}^{\prime}$-subunit absent $cgy_1cgy_1$, KTI protein present TiTi) parent. A total of 434 $F_2$ seeds were obtained and analyzed for the segregation of ${\alpha}^{\prime}$-subunit protein and KTI protein using SDS-PAGE. The segregation ratio of 3 : 1 for $Cgy_1$ locus (310 $Cgy_1$_ : 124 $cgy_1cgy_1$) and Ti locus (339 Ti_ : 95 titi) were observed. Segregation ratios of 9 : 3 : 3 : 1 (241 $Cgy_1$_Ti_: 69 $Cgy_1$_titi: 98 $cgy_1cgy_1$Ti_: 26 $cgy_1cgy_1titi$) between $Cgy_1$ gene and Ti gene in $F_2$ seeds were also observed (${\chi}^2= 5.367$, P = 0.10 - 0.20). This data showed that $Cgy_1$ gene was inherited independently with the Ti gene in soybean. These results will be useful in breeding program for selecting the line that does not exhibit or lacks both ${\alpha}^{\prime}$-subunit protein and KTI protein in soybean.

• Journal of Plant Biotechnology
• /
• v.45 no.4
• /
• pp.328-332
• /
• 2018

Soybean [Glycine max (L.) Merr.] seed is an important dietary source of protein, oil, carbohydrate, isoflavone and other various nutrients for humans and animals. However, there are anti-nutritional factors in the raw mature soybeans. Kunitz trypsin inhibitor (KTI) protein and stachyose are the main anti-nutritional factors in soybean seed. The ${\alpha}^{\prime}$-subunit of ${\beta}$-conglycinin protein exhibit poor nutritional and food processing properties. The genetic removal of the KTI and ${\alpha}^{\prime}$-subunit proteins will improve the nutritional value of the soybean seed. The objective of this research was to develop a new soybean strain with KTI and ${\alpha}^{\prime}$-subunit protein free ($titicgy_1cgy_1$ genotype) and proper agronomic traits. A breeding population was developed from the cross of the Bl-1 and 15G1 parents. A total of 168 $F_2$ seeds from the cross of the BL-1 and 15G1 parents were obtained. The segregation ratios of 9: 3: 3: 1 ($104Ti\_Cgy_{1\_}:\;30Ti\_cgy_1cgy_1:\;21cgy_1cgy_1Ti\_:\;13titicgy_1cgy_1$) between the Ti and $Cgy_1$ genes in the $F_2$ seeds were observed (${\chi}^2=5.12$, P=0.5-0.10). Two $F_4$ plant strains with proper agronomical traits and $titicgy_1cgy_1$ genotype (free of both KTI and ${\alpha}^{\prime}$-subunit protein) were selected and harvested. 2 strains (S1 and S2) had yellow seed coats and hilum. The plant height of the S1 strain was 65 centimeters. The 100-seed weight was 29.2 g. The plant height of the S2 strain was 66 centimeters and 100-seed weight was 26.2 g. The two strains selected in this research will be used to improve the new cultivar that will be free of the KTI and ${\alpha}^{\prime}$-subunit proteins.

• KOREAN JOURNAL OF CROP SCIENCE
• /
• v.57 no.1
• /
• pp.78-82
• /
• 2012

Soybean [$Glycine$ $max$ (L.) Merr.] protein is a high quality source for food and feed. But, antinutritional factors in the raw mature soybean are exist. Kunitz trypsin inhibitor (KTI) protein is a main antinutritional factor in soybean seed. Also, P34 protein, referred as $Gly$ $m$ Bd 30K, has been identified as a predominant immunodominant allergen. Genetic relationship between KTI protein and P34 protein could be useful in soybean breeding program for the genetic elimination or reduction of these factors. The objective of this study was to determine the independent inheritance or linkage between KTI protein and P34 protein in soybean seed. A total of 479 $F_2$ seeds were obtained from the cross of 07B1 and PI567476 parents. KTI protein and relative amount of P34 protein were analysed from $F_2$ seeds harvested from the F1 plants by using SDS-PAGE and Western blot analysis. The segregation ratios of 3 : 1 for KTI protein (353 KTI protein present : 126 KTI protein absent) and relative amount of P34 protein (363 normal amount of P34 protein : 116 low amount of P34 protein). The segregation ratio of 3 : 1 suggested that KTI protein and relative amount of P34 protein in mature soybean seed were controlled by a single major gene. The segregation ratios of 9 : 3 : 3 : 1 (266 KTI protein present, normal amount of P34 protein: 88 KTI protein present, low amount of P34 protein: 102 KTI protein absent, normal amount of P34 protein: 23 KTI protein absent, low amount of P34 protein) and Chi-square value (${\chi}^2$=3.31, P=0.346) were observed in $F_2$ seeds. This data showed that KTI protein was inherited independently with relative amount of P34 protein in soybean. These results will be helpful in breeding program for selecting the line with lacking KTI protein and reduced amount of P34 protein in soybean.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.25 no.4
• /
• pp.282-290
• /
• 1992

Based on surplus production models using fishery data for the last 20 years, a stock assessment was conducted for the small yellow croaker in Korean waters. The maximum sustainable yields (MSY) from the Schaefer and Fox models were estimated to be 37,000 metric tons (mt) and 33,450 mt. Zhang's model using time-series biomass with instantaneous coefficients of fishing mortality (F) and using time-series biomass and catch yielded MSY estimates of 45,328 mt and 40,160 mt, respectively. A yield-per-recruit analysis showed that the current yield per recruit of about 20g with F= 1.11 $yr^{-l}$, where the age at first capture $(t_c)$ is 0.604, was much lower than the maximum possible yield per recruit of 43g. Fixing $t_c$ at the current level and reducing fishing intensity (F) from 1.11 $yr^{-l}$ to 0.4 $yr^{-l}$ yielded only a small increase in predicted yield per recruit, from 20 to 25g. However, estimated yield per recruit increased to 43g by increasing $(t_c)$ from the current age (0.604) to age three with F fixed at the current level. This age at first capture corresponded to the optimal length which was obtained from the $F_{0.1}$ method. According to the analysis of stock recovery strategies employing the Zhang model, the optimum equilibrium biomass $(B^*_{MSY})$ which produces the maximum yield could be achieved after approximately five years at the lower fishing intensity (F=0.5).

• Applied Biological Chemistry
• /
• v.42 no.4
• /
• pp.310-316
• /
• 1999

BBPI contents in domestic soybean and soybean products were investigated by the measurement of chymotrypsin inhibiting activity(C.I.A) and competitive ELISA method. In order to produce polyclonal antibody, BBPI was purified from soybean trypsin-chymotrypsin inhibitor by ion exchange chromatography and electrophoretic gel slicing. Rabbit anti-BBPI polyclonal antibody was produced with the purified BBPI as immunogen. This antibody showed relatively specific binding to BBPI and then used for the establishment of competitive ELISA method to measure BBPI contents in extracts of soybean and soybean products. The standard curve for the measurement of BBPI in soybean extracts was drawn up within the range 0.03 to $30\;{\mu}g/ml$ of BBPI. The C.I.A. and BBPI contents of 12 soybean cultivars were $8,462{\sim}12,428\;U/g$ and $482{\sim}692\;mg%$, respectively. The C.I.A. and BBPI contents were not detected in most of soybean products except soybean sprouts, which contained $10,695{\sim}13,249\;U/g$ of C.I.A. and $529{\sim}803\;mg%$ of BBPI.