• Food Industry
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• s.118
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• pp.20-29
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• 1993

• Journal of the Korea Academia-Industrial cooperation Society
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• v.8 no.1
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• pp.156-166
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• 2007

Soybean meal was widely used as a protein source in pig feedstuff because it has a good amino acid balance compared with other vegetable sources. However, soybeans contain trypsin inhibitors and other antinutritional factors which can lead to lower the digestibility of amino acid, and consequently reduce the growth performance. Heat treatment of soybeans is helpful shown to decrease the antinutritional factors and elicit an improved growth performance. Additionally, microbial processe using(HP 100, HP 200 and HP 300), and non-protein constituent removal are suggested to improve the growth performance and nutrient digestibility. Inadequate heat treatment of soybeans gives no damage to adult pig, but it has been shown to decrease nutrient digestibility in young pig. So, soy protein concentrate (SPC) and Isolated soy protein(ISP) were more widely used for nursery pigs than growing and finishing pigs, since SPC and ISP have similar characteristics as milk product.

• Korean Journal of Breeding Science
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• v.41 no.4
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• pp.612-615
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• 2009

Lipoxygenase and Kunitz trypsin inhibitor protein are the main antinutritional factor in mature soybean seed. A new soybean cultivar, "Gaechuck#2" with yellow seed coat, lipoxygenase2,3-free and Kunitz trypsin inhibitor protein-free was developed. It was selected from the population derived from the cross between "Jinpumkong2ho" and C242. Plants of "Gaechuck#2" have determinate growth habit with purple flowers, tawny pubescence, yellow seed coat, yellow hilum, oval leaflet shape and brown pods at maturity. Seed protein and oil content on a dry weight basis were 40.7% and 18.7%, respectively. It has shown a resistant reaction to soybean necrosis, soybean mosaic virus, Cercospora leaf spot and blight, black root rot, pod and stem blight, and soybean pod borer. Gaechuck#2 matured in 4 October with plant height of 54cm and a 100-seed weight of 24.4g. Average Yield of Gaechuck#2 was 230 - 250 kg/10a in 2005 - 2007.

• Korean Journal of Breeding Science
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• v.40 no.2
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• pp.97-100
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• 2008

Lectin protein and Kunitz trypsin inhibitor (KTI) protein of mature soybean seed are a main antinutritional factor in soybean seed. The Le gene controls a lectin protein and Ti gene controls the KTI protein in soybean. Ti locus has been located on linkage group 9 in the classical linkage map of soybean. Position of Le locus on linkage map was not identified. Genetic relationship between Ti locus and Le locus could be useful in soybean breeding program for the genetic elimination of these factors. The objective of this study was to determine the independent inheritance or linkage between Ti locus and Le locus in soybean seed. Two $F_2$ populations were developed from three parents (Gaechuck#1, T102, and PI548415). The $F_1$ seeds from Gaechuck#1 (titiLeLe) ${\times}$ T102 (TiTilele) and Gaechuck#1 (titiLeLe) ${\times}$ PI548415 (TiTilele) were obtained. The lectin and KTI protein were analysed from $F_2$ seeds harvested from the $F_1$ plants to find independent assortment or linkage between Ti locus and Le locus. The segregation ratios of 3 : 1 for Le locus (129 Le_ : 44 lele) and Ti locus (132 Ti_ : 41 titi) and were observed. The segregation ratios of 9 : 3 : 3 : 1 (95 Le_Li_ : 34 Le_titi: 37 leleTi_ : 7 leletiti) between Le gene and Ti gene in $F_2$ seeds were observed. This data showed that Ti gene was inherited independently with the Le gene in soybean. These results will be helpful in breeding program for selecting the line with lacking both KTI and lectin protein in soybean.

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

• Journal of Microbiology and Biotechnology
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• v.24 no.10
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• pp.1413-1420
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• 2014

Phytate is an antinutritional factor that impacts the bioavailability of essential minerals such as $Ca^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$, and $Fe^{2+}$ by forming insoluble mineral-phytate salts. These insoluble mineral-phytate salts are hydrolyzed rarely by monogastric animals, because they lack the hydrolyzing phytases and thus excrete the majority of them. The ${\beta}$-propeller phytases (BPPs) hydrolyze these insoluble mineral-phytate salts efficiently. In this study, we cloned a novel BPP gene from a marine Pseudomonas sp. This Pseudomonas BPP gene (PsBPP) had low sequence identity with other known phytases and contained an extra internal repeat domain (residues 24-279) and a typical BPP domain (residues 280-634) at the C-terminus. Structure-based sequence alignment suggested that the N-terminal repeat domain did not possess the active-site residues, whereas the C-terminal BPP domain contained multiple calcium-binding sites, which provide a favorable electrostatic environment for substrate binding and catalytic activity. Thus, we overexpressed the BPP domain from Pseudomonas sp. to potentially hydrolyze insoluble mineral-phytate salts. Purified recombinant PsBPP required $Ca^{2+}$ or $Fe^{2+}$ for phytase activity, indicating that PsBPP hydrolyzes insoluble $Fe^{2+}$-phytate or $Ca^{2+}$-phytate salts. The optimal temperature and pH for the hydrolysis of $Ca^{2+}$-phytate by PsBPP were $50^{\circ}C$ and 6.0, respectively. Biochemical and kinetic studies clearly showed that PsBPP efficiently hydrolyzed $Ca^{2+}$-phytate salts and yielded myo-inositol 2,4,6-trisphosphate and three phosphate groups as final products. Finally, we showed that PsBPP was highly effective for hydrolyzing rice bran with high phytate content. Taken together, our results suggest that PsBPP has great potential in the animal feed industry for reducing phytates.