• Journal of Plant Biotechnology
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• v.47 no.3
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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.

• Journal of Animal Science and Technology
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• v.64 no.3
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• pp.500-514
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• 2022

The blood-epididymis barrier (BEB) forms a unique microenvironment that is crucial for the maturation, protection, transport, and storage of spermatozoa in the epididymis. To characterize the function of tight junctions (TJs), which are constitutive components of the BEB, we determined the expression and localization of TJ proteins such as zonula occludens (ZO)-1, 2, and 3, occludin, and claudin3 (Cldn3) during postnatal development in the goat epididymis. To assess the expression patterns of TJ proteins in immature (3 months of age) and mature (14 months of age) goat epididymides, two different experimental methods were used including immunofluorescence labeling and western blotting. We show that, ZO-1, 2, and 3, and occludin, were strictly expressed and localized to the TJs of the goat epididymis, whereas Cldn3 was present in basolateral membranes as well as TJs. All TJ proteins examined were more highly expressed in the immature epididymis compared to levels in mature tissue. In conclusion, our study indicates that at least five TJ proteins, namely ZO-1, ZO-2, ZO-3, occludin, and Cldn3, are present in TJs, and the expression strength and pattern of TJ proteins tend to be age dependent in the goat epididymis. Together, these data suggest that the distinct expression patterns of TJ proteins are essential for regulating components of the luminal contents in the epididymal epithelium and for forming adequate luminal conditions that are necessary for the maturation, protection, transport, and storage of spermatozoa in the goat epididymis.

• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.3
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• pp.55-61
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• 1987

This study was carried out to investigate the changes in the pH, extractability of protein, ATPase activity of myofibrillar protein, myofibrillar fragmentation, freezing loss and drip loss during storage at $4^{\circ}C$ and $-20^{\circ}C$ in breast and leg muscle of spent-hen meat. pH values ill pectoral and leg muscle were lowest ell tile 1st day and 1st week during cold and frozen storage, respectively. The extractabilities of myofibrillar proteins were increased graduall during cold storage and were highest on the 1st week during frozen storage, The $Mg^{2+}-ATPase$ activities of myofibrillar proteins were highest on the 1st day and 1st week during cold and frozen storage, respectively. The myofibrillar fragmentations were greatly changed on the 1st day during cold storage and 1st week during frozen storage. Freezing losses and drip losses were increased gradually during frozen storage. pH values in breast muscle were lower than those of leg muscle, and the extractabilities, $Mg^{2+}-ATPase$ activities, fragmentations of myofibrillar proteins, and drip losses in breast muscle were higher than those of leg muscle during storage, but the patterns of the changes in both muscles were similar during storage.

• Bulletin of the Korean Chemical Society
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• v.20 no.10
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• pp.1159-1164
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• 1999

The study investigated the effect of carrier composition (ionic strength and pH) on the retention of various proteins in flow field-flow fractionation (Flow FFF) as well as the conformational change of Bovine Serum Albumin (BSA) with urea concentration, storage time and temperature. The study found that the retention of protein in Flow FFF increased with the ionic strength of the carrier liquid. Most proteins were well solubilized at pH = 7-8. The hydrodynamic diameters obtained from Flow FFF retention data agree well with theoretical values. The retention increased and the peak shape became distorted at extreme pH conditions of the carrier solution. The selected carrier composition for comparison between the literature value of proteins was 0.05 M tris buffer solution with a pH of 8. Storing BSA at 4 ±2℃ over a period of three months resulted in slow dimerization. Also, in case of the storage of BSA at 37 ±5℃ for one week, the retention of both BSA monomer and dimer increased with the urea concentration. Finally, the structural composition of specific enzymes: malonyl-CoA decarboxylase (MCDC) and malonyl-CoA synthesis (MCS) was determined by using Flow FFF at specific carrier solutions. The molecular weight of the natural MCDC was determined to be 208 kDa, which means it is a homotetramer, while that of the MCS was determined to be 47 kDa, which means it is a monomer.

• Current Research on Agriculture and Life Sciences
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• v.31 no.2
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• pp.108-112
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• 2013

Nuts are one of the most common sources of allergies in individuals of all ages. In order for a particular protein to render an allergic reaction, it must resist proteolytic digestion by intestinal enzymes. In this study, three well-known allergenic nuts, almonds, cashew nuts, and peanuts, were used as samples, and enzyme digestion with Bacillus protease and porcine pepsin was tested. A proteomic approach using two-dimensional gel electrophoresis and an MS/MS analysis was applied to visualize and identify the proteins that were resistant to enzyme digestion. Among the 150 protein spots tested, 42 proteins were assigned functions. Due to the lack of genomic databases, 41% of the identified proteins were grouped as hypothetical. However, 12% of them were well-known allergens, including AraH. The remainder were grouped as storage, enzymes, and binding proteins.

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.06a
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• pp.293-293
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• 2017

The objective of this study was to determine physicochemical changes in brown rice during ageing condition. Five varieties (Haiami, Ilpum, Daecheong, Jungwon, and Dasan1) of brown rice were stored at $35^{\circ}C$ for 8 weeks. Crude protein and lipid content, seed germination rate, fat acidity, tocol content, TOYO glossiness value, pasting properties, and composition of storage proteins were measured to evaluate its quality during storage. The isomers of tocols (tocopherol and tocotrienols) were quantified using HPLC system, and the pattern of variation in rice storage proteins was examined through electrophoresis of protein extracts. Seed germination rate decreased by 2.7 times, whereas the fatty acid value dramatically increased by 4.8 times after 8 weeks of storage. Toyo glossiness value of cooked milled rice considerably affected by storage period, and the pasting properties of milled rice were also influenced by storage. The final viscosity and breakdown value increased, but setback decreased during storage. In terms of storage protein, proportion of prolamin (14.3 kDa) and globulin (26.4 kDa) increased, whereas percentage of glutelin (34-39 kDa and 21-22 kD) decreased. Furthermore, the contents of total tocol and isomers decreased in stored brown rice.

• Korean Journal of Food Science and Technology
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• v.38 no.1
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• pp.42-46
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• 2006

Rheological properties of the dough added with milk proteins and gums was studied to investigate the possibilities as anti-staling agents. Also, physical properties of the resultant bread baked from the frozen dough after 8 weeks of storage at $-20^{\circ}C$ were examined. The 4 sets of their combinations of milk proteins and gums, $casein-{\kappa}-carrageenan$ (CK), casein-sodium alginate (CA), $whey-{\kappa}-carrageenan$ (WK), and whey-sodium alginate (WA), were added to dough to examine their possible anti-staling effects. Rheological properties of dough were evaluated, and physical properties of resultant bread baked from frozen dough after 8 weeks storage at $-20^{\circ}C$ were examined. Addition of all treatments increased gelatinization temperature and water absorption, and lowered miximum viscosities and extension of doughs, compared to the control. Doughs added with CA and WA showed longer development times than that of the control. Addition of WK and WA resulted in lowest dough extensions. Treated bread showed lower moisture content decrease during storage at $5^{\circ}C$ for 4 days. Breads baked with frozen doughs after 6 weeks storage at $-20^{\circ}C$ showed similar results. Although textural hardness of breads increased with storage at $5^{\circ}C$, CA- and WA-added breads were less affected, showing they effectively retarded staling of breads.

• Korean Journal of Food Science and Technology
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• v.20 no.5
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• pp.650-658
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• 1988

The mobilization of proteins in the cotyledons of germinating soybean seeds (Glycine mar [L.] Merr.) and seedlings was studied by using light microscopy and transmission electron microscopy. The cotyledon tissues of soybean. were packed with protein bodies(diameter $0.1-15{\mu}m$) where storage protein of soybean is deposited. Degradation of protein bodies started in the epidermis and vascular tissues. After swelling of the protein bodies, autolysis of storage proteins began while the external membrane remained unbroken. Hydrolysis of proteins could be internal or peripheral and fusion might begin before complete protein degradation. Possible instances of vacuolar fusion were encountered in some cells. In all cases, the result of degradation was the same; the central vacuole of the cell. At the late stages of seedling growth, breakdown of tonoplast was observed in some cells.

• Proceedings of the Botanical Society of Korea Conference
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• 1987.07a
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• pp.261-282
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• 1987

Plants store a significant amount of their nitrogen, sulfur and carbon reserves as storage proteins in seed tissues. The major proteins present in rice seeds are the glutelins. Glutelins are initially synthesized at 4-6 days postanthesis and deposited into protein bodies via Golgi apparatus. Based on nucleic acid sequences and Southern blot analysis, the three isolated glutelin genomic clones were representative members of three gene subfamilies each containing 5 to 8 copies. A comparison of DNA sequences displayed by relevant regions of these genomic clones showed that two subfamilies, represented by clones, Gt1 and Gt2, were closely, related and probably evolved by more recent gene duplication events. The 5' flanking and coding sequences of Gt1 and Gt2 displayed at least 87% homolgy. In contrast, Gt3 showed little or no homolgy in the 5' flanking sequences upstream of the putative CAAT boxes and exhibited significant divergence in all other portions of the gene. Conserved sequences in the 5' flanking regions of these genes were identified and discussed in light of their potential regulatory role. The derived primary sequences of all three glutelin genomic clones showed significant homology to the legume 11S storage proteins indicating a common gene origin. A comparison of the derived glutelin primary sequences showed that mutations were clustered in three peptide regions. One peptide region corresponded to the highly rautable hypervariable region of legume peptide region of legume 11S storage proteins, a potential target area for protein modification. Expression studies indicated that glutelin mRNA transcripts are differentially accumulated during endosperm development. Promoterss of Gt2 and Gt3 were functional as they direct transient expression of chloramphenicol acetyltransferase in cultured plant cell.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.7
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• pp.903-907
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• 2006

Frozen stability of proteins recovered from white croaker and jack mackerel have been tested by measuring oxidation of residual lipid, browning, total plate count, and texture of gel during storage at $-20^{\circ}C$. The oxidation of residual lipid in recovered protein from Jack mackerel increased up to 60 days, and then decreased. Both browning values significantly was increased after 90 days. Total plate count was $1.2{\times}10^4\;CPU/g$ for proteins recovered from white croaker and $3.2{\times}10^4\;CPU/g$ for proteins recovered from jack mackerel in 60 days. The breaking force, deformation, and whiteness of gel formed from proteins recovered from white croaker did not change up th 120 days significantly, while proteins recovered from jack mackerel did not form heat-induced gel in 120 day. Frozen storage of the recovered protein was limited to 90 days for white croaker and to 60 days for jack mackerel considering the gelling ability and textural properties.