• 한국작물학회:학술대회논문집
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• 한국작물학회 2022년도 추계학술대회
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• pp.323-323
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• 2022

Jack bean [Canavalia ensiformis (L.)], belonging to the Leguminosae family has been frequently used in edible and medicinal plants in Asian countries. Jack beans are high in protein which is approximately 30%. Concanavalin A (Con A) is a major protein of Jack bean and belongs to the family of legume lectins. It has inhibitory effect on hepatocellular carcinoma by inducing autophagy. However, Con A negatively affects nutrient utilization by other mechanisms. It binds to the glycoproteins and glycolipids of the digestive tract mucosa, inhibits the activity of the enzymes of the brush border of the enterocytes. In order to use Jack bean young seedpods, they are restricted to 'young pods (soft, pre-swelling)' according to the 'Food Code' (Ministry of Food and Drug Safety). Therefore, in this study, we investigated the quantitative change of Con A across developmental stages of Jack bean pods. Biological samples consisted of Jack bean pods and seeds in 7 stages of development. The expression pattern of Con A mRNA was monitored by quantitative reverse transcription PCR (RT-qPCR). Expression of Con A proteins was analyzed by western blotting. The expression of Con A mRNA and protein in the seeds tended to increase gradually as the seeds expanded. However, in pods, they were much less than in seeds. As the expression of Con A mRNA and protein increases as the pods thicken, it is predicted that Con A synthesis increases when the thickness growth of the pod begins after the length growth of the pod is completed. Since the expression of Con A in the pods and seeds in very low when the pods are about 2 cm, therefore 2 cm pods seem appropriate when using 'young pods'. It is also necessary to study other proteins in Jack bean, such as Urease and Canavalin. These studies will serve as the basis for processing Jack bean.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2022년도 추계학술대회
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• pp.197-197
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• 2022

Wheat is highly susceptible to heat stress, which significantly reduces grain yield. In this study, we used RNA-seq technology to analyze the transcript expression at three different time-points after heat treatment in three cultivars differing in their susceptibility to heat stress: Jopum, Keumkang, and Olgeuru. A total of 11,751, 8850, and 14,711; 10,959,7946, and 14,205; and 22,895,13,060, and 19,408 differentially-expressed genes (log2 fold-change > 1 and FDR (padj) < 0.05) were identified in Jopum, Keumkang, and Olgeuru in the control vs. 6-h, in the control vs. 12-h, and in the 6-h vs. 12-h heat treatment, respectively. Functional enrichment analysis showed that the biological processes for DEGs, such as the cellular response to heat and oxidative stress-and including the removal of superoxide radicals and the positive regulation of superoxide dismutase activity-were significantly enriched among the three comparisons in all three cultivars. Furthermore, we investigated the differential expression patterns of reactive oxygen species (ROS)-scavenging enzymes, heat shock proteins, and heat-stress transcription factors using qRT-PCR to confirm the differences in gene expression among the three varieties under heat stress. This study contributes to a better understanding of the wheat heat-stress response at the early growth stage and the varietal differences in heat tolerancea.

• Journal of Nutrition and Health
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• 제56권6호
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• pp.589-601
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• 2023

Purpose: Baicalein, a natural flavone found in herbs, exhibits diverse biological activities. Nonalcoholic steatohepatitis (NASH) is an irreversible condition often associated with a poor prognosis. This study aimed to evaluate the effects of baicalein on the development of NASH in mice. Methods: Male C57BL/6J mice were randomly divided into four groups. Three groups were fed a methionine-choline-deficient (MCD) diet to induce NASH and were simultaneously treated with baicalein (at doses of 50 and 100 mg/kg) or vehicle only (sodium carboxymethylcellulose) through oral gavage for 4 weeks. The control group was fed a methionine-choline-sufficient (MCS) diet without the administration of baicalein. Results: The baicalein treatment significantly reduced serum levels of alanine aminotransferase and aspartate aminotransferase, suggestive of reduced liver damage. Histological analysis revealed a marked decrease in nonalcoholic fatty liver activity scores induced by the MCD diet in the mice. Similarly, baicalein treatment at both doses significantly attenuated the degree of hepatic fibrosis, as examined by Sirius red staining, and hepatocellular death, as examined by the terminal deoxynucleotidyl transferase dUTP nick end labeling assay. Baicalein treatment attenuated MCD-diet-induced lipid peroxidation, as evidenced by lower levels of hepatic malondialdehyde and 4-hydroxynonenal, demonstrating a reduction in oxidative stress resulting from lipid peroxidation. Moreover, baicalein treatment suppressed hepatic protein levels of 12-lipoxygenase (12-Lox) induced by the MCD diet. In contrast, baicalein enhanced the activities of antioxidant enzymes such as superoxide dismutase, catalase, and glutathione peroxidase. Additionally, baicalein treatment significantly reduced hepatic non-heme iron concentrations and hepatic ferritin protein levels in mice fed an MCD diet. Conclusion: To summarize, baicalein treatment suppresses hepatic lipid peroxidation, 12-Lox expression, and iron accumulation, all of which are associated with the attenuation of NASH progression.

• Journal of Microbiology and Biotechnology
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• 제34권2호
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• pp.233-239
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• 2024

N6-methyladenosine (m6A) RNA methylation has recently emerged as a significant co-transcriptional modification involved in regulating various RNA functions. It plays a vital function in numerous biological processes. Enzymes referred to as m6A methyltransferases, such as the methyltransferase-like (METTL) 3-METTL14-Wilms tumor 1 (WT1)-associated protein (WTAP) complex, are responsible for adding m6A modifications, while m6A demethylases, including fat mass and obesity-associated protein (FTO) and alkB homolog 5 (ALKBH5), can remove m6A methylation. The functions of m6A-methylated RNA are regulated through the recognition and interaction of m6A reader proteins. Recent research has shown that m6A methylation takes place at multiple sites within hepatitis B virus (HBV) RNAs, and the location of these modifications can differentially impact the HBV infection. The addition of m6A modifications to HBV RNA can influence its stability and translation, thereby affecting viral replication and pathogenesis. Furthermore, HBV infection can also alter the m6A modification pattern of host RNA, indicating the virus's ability to manipulate host cellular processes, including m6A modification. This manipulation aids in establishing chronic infection, promoting liver disease, and contributing to pathogenesis. A comprehensive understanding of the functional roles of m6A modification during HBV infection is crucial for developing innovative approaches to combat HBV-mediated liver disease. In this review, we explore the functions of m6A modification in HBV replication and its impact on the development of liver disease.

• 생명과학회지
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• 제22권4호
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• pp.559-564
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• 2012

식물생장과 발달에 중요한 역할을 하는 phytochrome이 ethylene 생합성에 미치는 영향을 조사하기 위하여 여러 빛 조건에서 키운 phyA, phyB, phyAB에서 ethylene 생합성과 생합성에 관여하는 enzyme activity를 측정하였다. White light에서 키웠을 때 모든 mutant에서 ethylene 생합성이 감소되었다. 특히 double mutant에서는 wild type과 비교하여 37%가 감소하였다. Dark에서 키웠을 때에는 wild type만 감소하였고, mutant에서는 감소효과가 나타나지 않았다. Red light에서 키웠을 때 double mutant에서 급격한 감소가 일어났다. Far-red light 에서 키웠을 때는 phyB만 감소가 일어나지 않았다. Ethylene 생합성에 관여하는 enzyme인 ACO 활성 패턴과는 달리ACS 활성 패턴은 ethylene 생성 패턴과 유사하게 나타났다. 이 결과를 바탕으로 ethylene 생합성에는 phytochrome A와 B 모두 중요한 작용을 하며 특히 $P_r$ 형태의 phytochrome이 ethylene 생성량을 조절한다는 것을 제시한다. 또한 phytochrome은 ethylene 생합성 단계에서 AdoMet가 ACC로 전환되는 단계에서 조절하는 것을 제시한다.

• Applied Biological Chemistry
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• 제50권4호
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• pp.308-315
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• 2007

오징어 가공 부산물인 오징어 내장을 효소제재와 같이 식품가공소재로 이용하기 위하여 오징어 내장의 endoprotease와 exopeptidase의 분포 특성에 대하여 살펴보았다. 오징어 내장은 조효소가 함유되어 있으리라 추정되는 단백질이 17.2%를 차지하였고, 또한, 이물질로 제거하여야 되는 조지방의 경우도 16.9%로 다량 차지하였다. 오징어 내장 조효소의 활성을 천연기질(azocasein)과 합성기질(LeuPNA 및 ArgPNA)로 나누어 살펴 본 결과 추출 용매(탈이온수, 1% NaCl, 1% KCl 및 1% NaCl-KCl 혼합용액)및 추출 시간(1-20시간)에 관계없이 전 조 효소가 동일 pH에서 천연기질의 분해활성에 비하여 상대적으로 합성기질의 분해활성(pH7.5)이 높아, 오징어 내장으로부터 효소를 분리하여 이용하고자 하는 경우 exopeptidase를 분리하여 이용하는 것이 적절하리라 판단되었다. 오징어 내장으로부터 exopeptidase를 분리하여 이용하고자 하는 경우 탈이온수를 이용하여 6-8시간 동안 추출하는 것이 가장 적절하리라 판단되었다. 오징어 내장 조효소의 최적 pH와 온도는 pH 7.5 및 $50-55^{\circ}C$범위로 판단되었다.

• 한국식품과학회지
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• 제49권2호
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• pp.215-221
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• 2017

다양한 영양성분을 함유할 뿐만 아니라 생리활성이 우수한 참죽으로부터 수용성 다당류를 추출하고 이들의 생리기능성을 측정하였다. 이를 위해 참죽을 열수, 초음파 및 효소(Viscozyme, Shearzyme)를 이용하여 수용성 다당류를 추출하고, 추출법에 따른 수용성 다당류의 기능성을 비교하였다. Searzyme 효소로 추출하여 얻은 수용성 다당류 분획의 수율과 총당 함량이 가장 높았다. 참죽으로부터 추출된 수용성 다당류 분획의 산화방지 활성을 측정한 결과, 열수추출에 의해 얻은 수용성 다당류 분획물의 $IC_{50}$ 값이 가장 낮게 나타나 가장 높은 산화방지 활성을 보였다. Tyrosinase 저해활성은 측정 농도가 증가할수록 모든 추출군의 활성이 증가하였다. 포도당 흡수지연 효과를 확인한 결과, 모든 추출군은 포도당 흡수 지연 효과를 보였으며, 특히, WSPs는 대조구인 CMC의 포도당 흡수지연 효과와 유사한 값을 나타내었다. Bile acid 흡수지연 효과를 측정한 결과, bile acid의 투과율이 CMC에 비해 높아 흡수지연 효과가 낮은 것으로 나타났다. 이상의 연구 결과, 열수에 의해 추출된 수용성 다당류분획이 뛰어난 산화방지 및 미백활성을 보였으며, Shearzyme 효소추출물이 우수한 포도당 흡수저해 효과를 보였다. 이를 통해 참죽으로부터 추출된 수용성 다당류는 향후 기능성 식품 소재로서의 개발 가능성이 높을 것으로 판단된다.

• Applied Biological Chemistry
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• 제4권
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• pp.17-22
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• 1963

원료배합(原料配合)을 다리한 간장용(用) 고일(一)지의 제국중(製麴中)에 있어서와 건조(乾燥)고일(一)지의 각종효소(各種酵素) activity 및 성분(成分)의 변화(變化)를 측정(測定)하여 다음결과(結果)를 얻었다. 1. 건조(乾燥)고일(一)지는 중성부근(中性附近)(pH 6.0)에 활성(活性)을 갖는 Protease가 주체(主體)를 이루며 산성(酸性) 및 alkali성측(性側)의 Protease activity는 이보다 미약(微弱)하고 밀을 많이 배합(配合)한 구(區)일수록 산성(酸性) 및 중성측(中性側) Protease activity가 높아지는 반면(反面)에 alkali성측(性側)은 이와 반대(反對)되는 경향(傾向)을 보였다. 2. 제국중(製麴中) 각종효소(各種酵素) activity는 모두 증가(增加)되었고 밀이 많은 배합구(配合區)일수록 ${\alpha}-Amylase$는 그 activity가 높아졌다. 3. 제국중(製麴中) 전당(全糖)은 감소(減少)되었으나 직당(直糖) 및 아미노 태질소(態窒素)와 전질소(全窒素)는 증가(增加)되었다. 4. 건조(乾燥)고일(一)지에 있어서 밀이 많은 배합구(配合區)일수록 직당(直糖) 및 전당(全糖)의 함량(含量)이 많어졌으나 전질소(全窒素)는 적어졌고 아미노(態窒素)는 차이(差異)가 없었다.

• Applied Biological Chemistry
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• 제46권2호
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• pp.84-89
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• 2003

$H^+-ATPase$ 활성을 조절할 수 있는 물질을 찾기 위하여 토마토 뿌리조직으로부터 마이크로솜을 분리하고 $La^{3+}$의 효과를 조사하였다. 원형질막 및 액포막에 위치하는 $H^+-ATPase$의 활성은 각각의 선택적 저해제인 vanadate와 $NO_3-$의 처리시 감소하여, $La^{3+}$이 원형질막 및 액포막 $H^+-ATPase$ 활성을 모두 저해함을 확인하였다. 원형질막과 액포막 $H^+-ATPase$ 활성을 50% 저해하는 $La^{3+}$ 농도인 Ki 값은 각각 57, $78\;{\mu}M$이었다. $La^{3+}$에 의한 저해효과는 Triton X-100을 처리한 leaky 마이크로솜에서도 얻어져, $La^{3+}$이 이온채널의 존재와 관계없이 $H^+-ATPase$의 활성을 직접적으로 저해함을 확인하였다. 한편, Lak의 활성저해 효과는 ATP 농도 증가로 감소하였고, ATP의 효과는 농도 의존적으로 나타났으며, 7 mM ATP 의해 $La^{3+}$에 의한 $H^+-ATPase$ 활성 저해가 완전히 억제되었다. 이러한 결과로부터 $La^{3+}$은 원형질막과 액포막의 $H^+-ATPase$들에 결합하여 ATP 결합친화력을 감소시킴으로써 활성을 저해하며, 뿌리조직 $H^+-ATPase$의 활성조절제로 이용이 가능함을 확인하였다.

• Journal of Microbiology and Biotechnology
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• 제17권10호
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• pp.1670-1674
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• 2007

Duffy binding protein (DBP) plays a critical role in Plasmodium vivax invasion of human red blood cells. We previously reported a single-chain antibody fragment (scFv) that was specific to P. vivax DBP (PvDBP). However, the stabilization and the half-life of scFvs have not been studied. Here, we investigated the effect of PEGylated scFvs on their biological activity and stability in vitro. SDS-PAGE analysis showed that three clones (SFDBII-12, -58, and -92) were formed as monomers (about 70 kDa) with PEGylation. Clone SFDBII-58 gave the highest yield of PEGylated scFv. Binding analysis using BIAcore between DBP and scFv showed that both SFDBII-12 and -58 were decreased approximately by two folds at the level of binding affinity to DBP after PEGylation. However, the SFDBII-92 clone still showed a relatively high level of binding affinity ($K_D=1.02{\times}10^{-7}\;M$). Binding inhibition assay showed that PEGylated scFv was still able to competitively bind the PvDBP and playa critical role in inhibiting the interactions between PvDBP protein expressed on the surface of Cos-7 cells and Duffy receptor on the surface of erythrocytes. When both scFvs and their PEGylated counterparts were exposed to trypsin, scFv was completely degraded only after 24 h, whereas 35% of PEGylated scFvs remained intact, maintaining their stability against the proteolytic attack of trypsin until 72 h. Taken together, these results suggest that the PEGylated scFvs retain their stability against proteolytic enzymes in vivo, with no significant loss in their binding affinity to target antigen, DBP.