• Title/Summary/Keyword: ${\beta}$-glycosidase

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Blood Glucose Lowering Activity and Mechanism of Supungsungihyan (SPSGH) in db/db Mouse (db/db 마우스에서 수풍순기환의 혈당강하 활성 및 기전연구)

  • 이성현;안세영;두호경;정성현
    • Biomolecules & Therapeutics
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    • v.7 no.4
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    • pp.335-341
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    • 1999
  • Antidiabetic activity and mechanism of Supungsungihyan(SPSGH) were examined in db/db mice, which is a spontaneously hyperglycemic, hyperinsulinemic and obese animal model. SPSGH and acarbose were administered orally for 4 weeks. Fasting and non-fasting serum glucose, glycated hemoglobin and trig-lyceride of SPSGH treated group were all reduced when compared with those of db/db control group. At 12th week after birth, SPSGH increased an insulin secretion although statistic significance was not seen. Total activities of sucrose, maltase and lactase in SPSGH treated group were not significantly different from those in db/db control. On the other hand, sucrase and maltase activities in acarbose treated groups were increased. Effect of SPSGH on mRNA expression of glucose transporter(GLUT-4) was also examined by RT-PCR and in vitro transcription with co-amplification of rat $\beta$-actin gene as an internal standard. Muscular GLUT-4 mRNA expression in SPSGH treated group was increased significantly. These results may suggest that SPSGH lowered blood glucose ascribing to upregulation of muscular GLUT-4 mRNA expression.

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The Effect of Cellulases on Flavonolglycosides of Ginkgo Leaf (은행잎 플라보놀배당체에 대한 셀루라제류의 영향)

  • 배기환;민병선;백흠영;안병준
    • YAKHAK HOEJI
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    • v.35 no.4
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    • pp.271-276
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    • 1991
  • The extractability and stability of ginkgoflavonolglycosides under presence of several cellulose preparations were investigated. The enzymes used were macerosin, cellulose C and cellulase NC. The content variation of the glycosides was measured with HPLC method, using caffeic acid as an internal standard. The methanol extract of ginkgo leaf, containing the total flavonolglycosides of 4.46%, was used for the content comparison. By extraction with the enzymes, each or mixed, the peak levels of all the glycosides began to decrease after 1 or 2 hours. After 24 hour extraction, most of the glycosides were degraded to minor components. The flavonolglycosides in ginkgo leaf were also hydrolysed simply by the water extraction. After 24 hour extraction with water at $40^{\circ}C$, the peak levels of major glycosides were distinctly decreased. Rutin was hydrolysed by enzyme treatment or by ginkgo leaf itself. As a result, it was concluded that the commercially available cellulases and the ginkgo leaf itself contain the activities of $\beta$-glycosidase and $\alpha$-rhamnosidase. Kaempferol-3-O-(6'"-O-p-coumaroylglucosyl)-rhamnoside and four other ginkgo flavonolglycosides were not hydrolysed under the same condition.tion.

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Antiviral activity of methanol extract from Rhus chinensis gall (오배자 추출물의 항바이러스 활성)

  • Lee, Doseung;Min, TaeSun;Lee, Dong-Sun
    • Journal of Applied Biological Chemistry
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    • v.61 no.4
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    • pp.379-382
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    • 2018
  • Trafficking process of viral glycoprotein to cell surface results in the syncytium formation when baby hamster kidney (BHK) cells was infected by Newcastle disease virus (NDV). Rhus chinensis gall, well-known as a medicinal plant, inhibited not only syncytium formation, but also trafficking of glycoprotein, hemagglutinin-neuramidase (HN) to the cell-surface. Modification of viral glycoprotein is processed within the endoplasmic reticulum and golgi body during trafficking into surface. R. chinensis gall extracts showed the strong inhibitory activities ($IC_{50}$ $12.5{\mu}g/mL$) against ${\alpha}-glucosidase$, when compared with the ${\beta}-glucosidase$. And this inhibitory activities is increased by the samples in a dose-depedent pattern. These data showed that the extracts of R. chinensis gall inhibited the cell-surface expression of NDV-hemagglutinin-neuramidase glycoprotein without significantly affecting HN glycoprotein synthesis in NDV-infected BHK cells.

Enhanced Antioxidant Effect of Black Soybean by Cheonggukjang with Potential Probiotic Bacillus subtilis CSY191 (잠재적인 생균제제 Bacillus subtilis CSY191에 의한 검정콩 청국장의 항산화 증진 효과)

  • Hwang, Chung Eun;Seo, Weon Taek;Cho, Kye Man
    • Korean Journal of Microbiology
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    • v.49 no.4
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    • pp.391-397
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    • 2013
  • Changes in ${\beta}$-glycosidase activity, total phenolic and isoflavone contents, and antioxidant activities during the fermentation of Korean black soybeans (Seoritae and Seomoktae) fermented food cheonggukjang by the potential probiotic Bacillus subtilis CSY191 were investigated. The levels of total phenolic and isoflavone-malonylglycoside and -aglycone contents increased, while 2,2-azinobis (3-ethyl-benzothiazoline-6-sulfonic acid) diammonium salt (ABTS) radical scavenging activity and ferric reducing/antioxidant power (FRAP) increased, but the isoflavone-glycoside contents decreased after cheonggukjang fermentation. The content of antioxidant compounds, including isoflavone-aglycones and -malonylglycosides, was increased by fermenting-processing, whereas the content of isoflavone-glycosides was decreased in the fermented soybeans. In particular, the Seoritae soybean fermented at 3 $7^{\circ}C$ for 48 h displayed the highest antioxidant activities, compared to those of the Seomoktae soybean and the fermented. The highest levels of daidzein, glycitein, and genistein were present at concentrations of 253.0 ${\mu}g/g$, 72.5 ${\mu}g/g$, and 114.1 ${\mu}g/g$ after 48 h of Seoritae soybean fermentation. From those results, we suggest that the high antioxidant activity of cheonggukjang of black soybeans might be related to the markedly higher levels of total phenolic and isoflavone-aglycone and -malonylglycoside contents achieved during fermentation.

A comparison of the hydrolase activities of excretory-secretory products and somatic extracts from fish parasitic nematodes, Anisakis simplex sensu stricto and Anisakis pegreffii larvae (어류 기생성 선충 Anisakis simplex sensu stricto와 Anisakis pegreffii 유충의 excretory-secretory products 및 somatic extracts의 가수분해효소 활성 비교)

  • Jeon, Chan-Hyeok;Wi, Seong;Kim, Jeong-Ho
    • Journal of fish pathology
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    • v.27 no.1
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    • pp.25-33
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    • 2014
  • Hydrolase activities of excretory-secretory products (ESP) and somatic extracts (SE) from Anisakis simplex sensu stricto (s.s.) and Anisakis pegreffii larvae were investigated by using API ZYM kit. In esterase group, acid phosphatase showed high activity from both of A. simplex (s.s.) and A. pegreffii. Esterase (C4) showed activity only from SE and A. simplex (s.s.) showed higher activity than A. pegreffii. Alkaline phosphatase, acid phosphatase and naphthol-AS-BI-phosphohydrolase showed higher activity in 3rd stage larvae than in 4th stage larvae of both species. In aminopeptidase group, only leucine arylamidase showed remarkable activity in SE of both anisakid species, and A. simplex (s.s.) SE showed higher activity than A. pegreffii SE. In glycosidase group, N-acetyl-${\beta}$-glucosaminidase, ${\alpha}$-mannosidase, ${\alpha}$-fucosidase showed higher activity in A. simplex (s.s.) than A. pegreffii, and 4th larvae showed higher activity than 3rd larvae. These differences in hydrolase activity of anisakid nematodes larvae are thought to be due to different metabolism such as growth, moulting, digestion and feeding.

Influence of Gibberellic Acid on α-D-Galactosidase Activity in the Grape Berry

  • Kang, Han-Chul;Lee, Seon-Hwa;Kim, Jong-Bum
    • Journal of Applied Biological Chemistry
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    • v.44 no.2
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    • pp.53-58
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    • 2001
  • Glycosidase activities in the grape flesh (Marguerite) were assayed, and the order of activity was marked as follows: ${\alpha}$-D-galactosidase>${\alpha}$-D-mannosidase>${\alpha}$-D-glucosidase>${\beta}$-D-galactosidase>${\beta}$-D-glucosidase. Of these glycosidases, ${\alpha}$- and ${\beta}$-D-galactosidases were prominently expressed by the treatment of gibberellic acid, resulting in 56 and 238% increase of activity, respectively. Most of ${\alpha}$-D-galactosidase was found in the flesh texture, and the activity increase by gibberellic acid occurred mostly in this tissue. The increase in ${\alpha}$-D-galactosidase activity was dependent on the concentration of gibberellic acid treated, showing a positive correlation. Gibberellic acid affected the content of total protein in the grape flesh, 49% increase by 75 ppm treatment. Above this concentration, higher gibberellic acid level did not influence the protein expression. Specific activity of the ${\alpha}$-D-galactosidase still increased, showing 24% increase in activity. Grape flesh subjected by gibberellic acid (100 ppm) resulted in the increased activity against a natural substrate, stachyose, showing 55% increase in activity from the grapes treated with 100 ppm of gibberellic acid. Other natural substrates, such as melibiose and raffinose, were also considerably hydrolyzed, and the extent was similar to that of stachyose hydrolysis. During postharvest storage, ${\alpha}$-D-galactosidase activity in the grape flesh increased by 51% after 20 days and then declined slowly.

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Antiviral activity of methanol extract from Ephedra sinica Stapf (마황 추출물의 항바이러스 활성)

  • Lee, Doseung;Lee, Dong-Sun
    • Food Science and Preservation
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    • v.21 no.5
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    • pp.735-739
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    • 2014
  • Ephedra sinica Stapf, known as a medicinal plant, inhibited not only syncytium formation, but also trafficking of viral glycoprotein, hemagglutinin-neuramidase (HN) to the cell-surface. Trafficking of viral glycoprotein to the surface of infected-cells results in syncytium formation in Newcastle disease virus (NDV)-infected baby hamster kidney (BHK) cells. Viral glycoprotein in the infected-cell is processed within the endoplasmic reticulum during routing into surface. The processing of viral glycoprotein like a N-linked oligosaccharide trimming by ${\alpha}$-glucosidase in cell is necessary for virus infection. Methanol extracts showed inhibitory activities ($IC_{50}$ $15{\mu}g/mL$) against ${\alpha}$-glucosidase. This suggested that E. sinica extracts inhibited the cell-surface expression of NDV-HN glycoprotein without significantly affecting HN glycoprotein synthesis in NDV-infected BHK cells.

Identification of Alga-lytic Bacterium AK-07 and Its Enzyme Activities Associated with Degradability of Cyanobacterium Anabaena cylindrica (Anabaena cylindrica 분해세균 AK-07의 동정과 분해 관련 효소활성 조사)

  • Kim, Jeong-Dong;Han, Myung-Soo
    • Korean Journal of Ecology and Environment
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    • v.36 no.2 s.103
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    • pp.108-116
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    • 2003
  • To investigate bacteria with algal Iytic activities against Anabaena cylindrica when water blooming occurs and to study enzyme profiles of alga-Iytic bacteria, various bacterial strains were isolated from surface waters and sediments in eutrophic lakes or reservoirs in Korea. Abacterial strain AK-07 was characterized and identified as Acinetobacter johnsonii based on its16S rDNA base sequence. When AK-07 was co-cultivated with A. cylindrica, bacterial cells propagated to $8\;{\times}\;10^8$ cfu $ml^{-1}$ and Iyses algal cells. However, culture filtrates of AK-07 did not exhibit algal Iytic activities. That suggesting the enzymes on the surfaces of the bacterium might be effective algal Iytic agents to cause Iyses of cells. Acinetobacter johnsonii AK-07 exhibited high degradation activities against A. cylindrica, and formed alginase, caseinase, lipase, fucodian hydrolase, and laminarinase. Moreover, glycosidases for example ${\beta}$-galatosidase, ${\beta}$-glucosidase, ${\beta}$-glucosaminidase, and ${\beta}$-xylosidase, which hydrolyzed ${\beta}$-0-glycosidic bonds, were found in cell-free extracts of A. johnsonii AK-07. Other glycosidase such as ${\alpha}$-galctosidases, ${\alpha}$-N-Ac-galctosidases, ${\alpha}$-mannosidases, and ${\alpha}$- L-fuco-sidases, which cleavage ${\alpha}$-0-glycosidic bondsare not detected. In the results, enzyme systemsof A. johnsonii AK-07 were very complex to do-grade cell walls of cyanobacteria. The polysaccharides or peptidoglycans of A. cylindrica maybe hydrolyzed and metabolized to a range of easily utilizable monosaccharides or other low molecular weight organic substances by strain AK-07 of A. johnsonii.

Enzymatic N-glycan analysis of 31 kDa molecule in plerocercoid of Spirometra mansoni (sparganum) and its antigenicity after chemical oxidation

  • Chung, Young-Bae;Kong, Yoon;Yang, Hyun-Jong
    • Parasites, Hosts and Diseases
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    • v.42 no.2
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    • pp.57-60
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    • 2004
  • A highly specific antigenic protein of 31 kDa from plerocercoid of Spirometra mansoni (sparganum) was obtained by gelatin affinity and Mono Q anion-exchange column chromatography. The purified 31 kDa protein was subjected to N-glycan enzymatic digestion for structural analysis. The relative electrophoretic mobility was analyzed by SDS-PAGE, before and after digestion. On SDS-PAGE after enzymatic digestion, the 31 kDa protein showed a molecular shift of approximately 2 kDa, which indicated the possession of complex N-linked oligosaccharides (N-glycosidase F sensitive) but not of high-mannose oligosaccharides (endo-beta-N-acetylglucosaminidase H, non-sensitive). Chemically periodated 31 kDa protein showed statistically non-significant changes with human sparganosis sera by enzyme linked immunosorbent assay (ELISA). Therefore, the dominant epitopes of the 31 kDa molecule in human sparganosis were found to be mainly polypeptide, while N-glycans of the antigenic molecule in sparganum was minimal in anti-carbohydrate antibody production.

ISOLATION OF A NEW $\alpha$-GLUCOSIDASE INHIBITOR FROM A FUNGUS, PENICILLIUM SP. F70614

  • Kwon, Oh-Sung;Park, Sang-Ho;Lee, Sang-Hwa;Park, Dong-Jin;Yun, Bong-Sik;Kim, Chang-Jin
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1998.11a
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    • pp.134-134
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    • 1998
  • The modulation of glycosidase activity by inhibitors is of great interest. Such compounds have been shown to be important tools in mechanistic studies on glycohydrolase as well as having promising therapeutic application. An ${\alpha}$-glucosidase inhibitor was isolated from culture filterates of Penicillium sp. The inhibitor was active against ${\alpha}$-glucosidase isolated from yeast and porcine small intestine. However, it showed no inhibition to Aspergillus ${\alpha}$-galactosidase, Escherichia coli ${\beta}$-galactosidase, and jack bean ${\alpha}$-mannosidase. The inhibitor was highly soluble in ether, methanol and chloroform. The inhibitor was purified using silica gel, Sephadex LH-20 column chromatography and reverse-phase HPLC. The inhibitory compound designated PA-7(IC$\sub$50/=35$\mu\textrm{g}$) was obtained as white powder. The structure of PA-7 was determined with spectroscopic data of EI-MS, FAB-MS, $^1$H, and $\^$13/C NMR. The inhibitor has a diketopiperazine moiety.

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