• Journal of Applied Biological Chemistry
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• v.66
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• pp.289-298
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• 2023

Stored rice grain undergoes physical and chemical deteriorations over time. As temperature and moisture content are important factors affecting to the denaturation of rice, it is important to store rice at a low temperature and hermetic condition. From a microscopic point of view, many studies have already reported how proteins and lipids were denatured within rice grain. Meanwhile, the weight loss of rice is currently observed at actual storage sites and can occur for diverse reasons. In this study, it was assumed that the decomposition process of polysaccharides, known as the main component of rice, plays an important role in its weight loss. In specific, the roles of enzymes were also evaluated. Our interest is in the major polysaccharides within a rice grain such as starch as well as within a rice endosperm cell wall. It is suspected that the weight loss of rice grains during storage seems to associate with the degradation of amylose and amylopectin. Nevertheless, it should be also speculated the correlating effect of other components such as proteins and lipids.

• Journal of Plant Biotechnology
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• v.38 no.4
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• pp.263-271
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• 2011

Rice is one of the most important food crops since it is consumed by approximately 60% of the world's population. The most abundant component of rice grain is starch that is an important source of energy. The second abundant component is protein, which is an important protein source for people in many developing countries that rarely take animal protein. However, the rice protein lacks the essential amino acid lysine. Therefore, nutritional improvement in the essential amino acid composition of rice proteins is required. On the other side, rice grain has attracted attention as a diet and health food in developed countries, because its proteins have superior physiological and food processing properties. Thus, nutritional improvements in rice seed proteins by changing amino acid composition or introducing an useful protein or peptide have been studied. This review aims at assessing the current research status of biosynthesis, accumulation, genetic improvement of seed storage proteins by mutation or genetic engineering in rice.

• Food Science and Preservation
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• v.21 no.6
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• pp.776-783
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• 2014

Kimchi cabbages were cut ($3{\times}3cm$), and were pre-heat treated at $40^{\circ}C$, and their physicochemical qualities and browning degrees were investigated during 8 weeks storage at $5^{\circ}C$. The Cut kimchi cabbages were treated at $40^{\circ}C$ (1~8 hrs) and their protein bands profiles were determined by sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE). The 60, 39, 33, and 12 kDa bands considered heat shock proteins (HSPs) were expressed in the cut kimchi cabbage, and the 4-hr pre-heat treatment (HS 4) exhibited the strongest band ratio. The weight ratios and titratable acidities of the pre-heat treated cut kimchi cabbages were not changed so much after 8 weeks storage at $5^{\circ}C$, and the soluble solid contents of HS 4 decreased less than that of any other treatments. The browning degree of HS 4 after 8 week storage was also shown to be the least among the treatments. The polyphenol oxidase (PPO) activities of all treatments slightly rose during the over all storage period, in contrast with the decrease of total phenolic contents. The expression of HSPs was identified in the pre-heat treated cut kimchi cabbages, and HS 4 exhibited the best quality and appearance after 8 weeks storage at $5^{\circ}C$.

• Journal of Life Science
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• v.33 no.7
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• pp.586-592
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• 2023

Oxidative stress is a critical factor affecting the quality and viability of sperm during boar semen storage. Oxidative stress is also a significant concern during the process of freezing semen. The process of semen storage involves exposing the sperm to various stressors, including temperature changes, cryoprotectants, and extended periods of incubation. In addition, oxidative stress can lead to the production of reactive oxygen species (ROS) within the sperm, resulting in oxidative damage to cellular components, such as lipids, proteins, and DNA. Striking a balance between ROS production and the antioxidant defense system is crucial for maintaining sperm viability and functionality during semen storage. Moreover, the prolonged storage of boar semen leads to an increase in ROS levels, which can impair sperm motility, membrane integrity, and DNA integrity. ROS-induced lipid peroxidation affects the fluidity and stability of sperm membranes, leading to decreased sperm motility. Moreover, oxidative damage to the DNA can result in DNA fragmentation, compromising the genetic integrity of the sperm. In conclusion, oxidative stress is a significant challenge in maintaining sperm quality during boar semen storage. Understanding the mechanisms underlying oxidative stress and their impacts on sperm function is crucial for developing effective strategies to minimize oxidative damage and improve sperm storage outcomes.

• Journal of Plant Biotechnology
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• v.8 no.1
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• pp.1-8
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• 2006

The differential response of soybean cultivars with or without sulfur (S) application was observed under fold conditions. Plant biomass decreased by sulfur deficiency but the reduction was less in Bragg variety about 26 % relative to the control than other ones over 45%, probably due to less reduction in loaves and pods. The photosynthetic rate of Bragg cultivar was also unaffected by the absence of sulfur application while it depressed in other lines. Soybean cultivars were compared in terms of storage protein, protein quality and biomass production by application of sulfur nutrition. The storage protein concentration tended to decrease without sulfur application in all the cultivars, however the differential response of protein quality only by 11S/7S ratio to sulfur nutrition status was observed: For instance, Bragg cultivar had higher biomass and protein production but protein quality decreased at sulfur deficiency. On the other hand, biomass and protein production in other cultivars remained louver at sulfur deficiency but protein quality differed genetically in spite of sulfur nutrition status. These results suggest that the response of soybean to sulfur nutrition is controlled by genotypic difference and sulfur supply status.

• Food Science and Biotechnology
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• v.17 no.5
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• pp.912-918
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• 2008

This study was conducted to identify the differences in proteomic characteristics of 'Agakong', recombinant inbred line, and its parental genotypes 'Eunhakong' (Glycine max) and 'KLG10084' (G. soja). The isoflavone content of 'Agakong' was 3 times higher than that of its parental lines. A combined high-throughput proteomic approach was employed to determine the expression profile and identity of proteins using 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. The overall distribution patterns of proteins are quite similar, but lots of protein spot intensities varied among the genotypes. A total of 41 proteins, representing significant difference in the quantities of protein among the lines, were successfully identified. Among them, more than 50% of the proteins identified were subunits of glycinin and $\beta$-conglycinin, 2 major storage proteins. This study showed that the proteomic analysis could help to define specific changes in protein level and composition, which can occur in the generation of new soybean varieties.

• Korean Journal of Plant Tissue Culture
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• v.27 no.4
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• pp.339-343
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• 2000

When plants are exposed to subfreezing temperatures ice crystals are forming within extracelluar space in leaves. The growth of ice crystal is closely related to the degree of freezing injury. It was shown that an antifreeze protein binds to an ice nucleator through hydrogen bonds to prevent growth of ice crystal and also reduces freezing damage. The antifreeze proteins in plants are similar to PR proteins but only the PR proteins induced upon cold acclimation were shown to have dual functions in antifreezing as well as antifungal activities. Three of the genes encoded for CLP, GLP, and TLP were isolated from barley and Kentucky bluegrass based on amino acid sequence revealed after purification and low temperature-inducibility as shown in analysis of the protein. The deduced amino acid of the genes cloned showed a signal for secretion into extracellular space where the antifreezing activity sup-posed to work. The western analysis using the antisera raised against the antifreeze proteins showed a positive correlation between the amount of the protein and the level of freeze tolerance among different cultivars of barely. Besides it was revealed that TLP is responsible for a freeze tolerance induced by a treatment of trinexapac ethyl in Kentucky bluegrass. Analysis of an overwintering wild rice, Oryza rufipogon also showed that an acquisition of freeze tolerance relied on accumulation of the protein similar to CLP. The more direct evidence for the role of CLP in freeze tolerance was made with the analysis of the transgenic tobacco showing extracellular accumulation of CLP and enhanced freeze tolerance measured by amount of ion leakage and rate of photosynthetic electron transport upon freezing. These antifreeze proteins genes will be good candidates for transformation into crops such as lettuce and strawberry to develop into the new crops capable of freeze-storage and such as rose and grape to enhance a freeze tolerance for a safe survival during winter.

• Journal of Microbiology and Biotechnology
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• v.30 no.2
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• pp.259-270
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• 2020

Listeria monocytogenes is a gram-positive, facultative anaerobe food pathogen responsible for the listeriosis that mostly occurs during the low-temperature storage of a cold cut or dairy products. To understand the systemic response to a wide range of growth temperatures, L. monocytogenes were cultivated at a different temperature from 10℃ to 42℃, then whole cell proteomic analysis has been performed both exponential and stationary cells. The specific growth rate increased proportionally with the increase in growth temperature. The maximum growth rate was observed at 37℃ and was maintained at 42℃. Global protein expression profiles mainly depended on the growth temperatures showing similar clusters between exponential and stationary phases. Expressed proteins were categorized by their belonging metabolic systems and then, evaluated the change of expression level in regard to the growth temperature and stages. DnaK, GroEL, GroES, GrpE, and CspB, which were the heat&cold shock response proteins, increased their expression with increasing the growth temperatures. In particular, GroES and CspB were expressed more than 100-fold than at low temperatures during the exponential phase. Meanwhile, CspL, another cold shock protein, overexpressed at a low temperature then exponentially decreased its expression to 65-folds. Chemotaxis protein CheV and flagella proteins were highly expressed at low temperatures and stationary phases. Housekeeping proteins maintained their expression levels constant regardless of growth temperature or growth phases. Most of the growth related proteins, which include central carbon catabolic enzymes, were highly expressed at 30℃ then decreased sharply at high growth temperatures.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.43 no.4
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• pp.228-233
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• 1998

Seed storage proteins have been used for studying biochemical genetics and end-use quality aspects. We conducted enzyme-linked immunosorbent assay (ELISA) and one-dimensional SDS-PAGE (1D SDS-PAGE) to evaluate different cereal crop species and Korean wheat lines for rye secalin proteins. The antisecalin antibody showed consistent specificity for rye secalin with little cross-reactivity to gliadins. Immunological cross-reactivities measured by the ELISA technique using competition assay showed significant differences of absorbance among rye, triticale, wheat-rye translocated wheat and non-translocated wheat. The absorbance values were lowest in rye followed by triticale, translocated wheat and non-translocated wheat. The ELISA for discrimination of wheat-rye translocation on the basis of antigen-antibody reactivity showed that none of the Korean wheat lines possessed 1RS and secalin proteins. The competitive ELISA experiment demonstrated specific determination for secalin that was originated from rye chromosomal parts. The result of 1D SDS-PAGE for identifying rye secalin subunits showed all three rye specific secalin protein subunits (75 KDa, 45 KDa, and 40 KDa) for rye and triticale, and 1RS specific secalins (45 KDa and 40 KDa) for 1AL/1RS and 1BL/1RS translocated wheats. All Korean wheats were lacking 1RS of rye chromosome and secalin.

• Archives of Pharmacal Research
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• v.21 no.6
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• pp.629-633
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• 1998

In addition to selecting proteins for degradation by the 26S proteasome, ubiqitination appears to serve other regulatory functions, including for endosomal/lysosomal targeting, protein translocation, and enzyme modification. Currently, little is known how multiubiquitin chains are recognized by these cellular mechanisms. Within the 26S proteasome, one subunit (Mcb1/S5a) has been identified that has affinity for multiubiquitin chains and may function as a ubiquitin receptor. We recently found that a non-proteasomal protein p62 also preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure "sequestosome" which serves as a storage place for ubiquitinated proteins. In the present manuscript, the role and regulation of p62 in relation to the sequestosomal function will be reviewed.