• Microbiology and Biotechnology Letters
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• v.28 no.2
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• pp.92-96
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• 2000

Aspergillus sp. F184 was isolated from soil for the development of new xanthine oxidase inhibitor. This xanthine oxidase inhibitor was sequentially purified by filtration, HP-20 adsorption column chromatography, ethyl acetate extraction, silica gel column chromatography and crystallization, and was named as YUX 104. YUX 104 was identified to be 5,6-epoxy-2-hydroxy-3-methyl-2-cyclohexene-1,4-dione(terreic acid) by NMR and mass spectroscopic sudies.

• Korean Journal of Plant Resources
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• v.21 no.1
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• pp.12-18
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• 2008

Antioxidative activity and inhibitory activity of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase were investigated in the methanol extracts from 25 fern plants native to Jeju Island, in order to screen the plant species containing bioactive materials for functional foods or medicines. The antioxidative activity was higher in Cytomium fortunei(41.9%) and Rumohra standishii(34.1%) than in leaves of Thea sinensis(30.9%), a small tree for antioxidative beverage. Inhibitory activities of ACE and APN were relatively high in Cytomium fortunei as 26.7% and 28.2% respectively. $\alpha$-Amylase inhibitory activity was higher than 50% in 10 species. Particularly, Cytomium fortunei(87.4%) and Dryopteris erythrosora(71.6%) showed the inhibitory activities higher than those of other form plants. Of 25 fern plants investigated here, Cytomium fortunei showed not only the highest antioxidative activity but also the highest inhibitory activity of ACE, APN and $\alpha$-amylase. It suggests that Cytomium fortunei could be potentially used as a resource of bioactive materials for fuctional foods or medicines.

• Journal of Life Science
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• v.18 no.2
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• pp.273-278
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• 2008

Various biological resources from plants, animals, mushrooms, microorganisms, and foods were tested for the inhibitory activity against squalene synthase (SQS). Among 32 samples, more than one fourths (9 samples) exhibited significant SQS inhibitory activity. Interestingly, SQS inhibitory activity was detected in the samples such as green tea, fermented soybean paste, and plum juice. The SQS inhibitory activity of green tea was not only high but also stable. Its SQS inhibitors were supposed to be catechin derivatives, which have been known to be main bioactive components in green tea. The galloyl catechins showed higher SQS inhibitory activity compared to the nongalloyl catechins. Especially, (-)-epigallocatechin gallate appeared to be strongest inhibitor against squalene synthase ($IC_{50}=90{\mu}M$).

• The Korean Journal of Food And Nutrition
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• v.19 no.4
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• pp.526-531
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• 2006

Minimum inhibition concentration(MIC), growth inhibition activity, and colony forming inhibitory activity of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enterifidis and Serratia marcescens were tested. MIC of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was 12.5, 12.5, 12.5, 50, 50, 100ppm, respectively. Growth inhibition concentration of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was below 1.0, 6.25, below 1.0, 6.25, 25, 25ppm, respectively. Colony forming inhibitory activity of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was 93.9, 94.0, 99.9, 4.4, 82.7, 86.4%, respectively. Colony forming inhibitory activities of grapefruit seed extract against Gram positive bacteria were higher than that against Gram negative bacteria.

• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.501-505
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• 1990

Streptomyces sp. KISl3 isolated from soil was found to produce low molecular weight thiol protease inhibitors. The protease inhibitor production was closely linked to the cell growth and regulated by growth condition. The inhibitor was purified from the culture broth through butanol extraction, silicagel 60 column chromatography, Sephadex LH-20 gel filtration and preparative HPLC. The inhibitor showed specific inhibitory activity to thiol protease such as papain, picin and bromelain. The mode of inhibition against papain to Hammersten casein as a substrate was non-competitive.

• Applied Biological Chemistry
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• v.47 no.1
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• pp.149-153
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• 2004

전통된장 제조방법으로서 원료 혼합비, 메주의 건조시간 및 온도, 메주와 된장의 발효 시간 및 온도, 된장 간장의 분리 여부, 된장 숙성(aging) 시간을 조사하였다. 혈액응고 저해 활성(anticoagulant activity)을 fibrin clotting assay법으로 분석하여 혈액응고 저해활성과 제법간의 상관 관계를 검토하였다. 숙성 기간이 길수록 혈액응고 저해활성이 높게 나타나는 경향을 보였으나 선형적인 상관관계보다는 비선형적으로 양의 상관관계를 갖는 것으로 판단되었다. 이상의 결과를 토대로 혈액응고 저해활성이 높은 2종의 된장시료를 선발하였으며 숙성기간이 180일 이상일 경우 전통된장의 혈액응고 저해활성이 높은 것으로 판단되었다.

• Korean Journal of Microbiology
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• v.28 no.1
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• pp.65-70
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• 1990

The objective of the current study is to elucidate the biological roles of proteinase inhibitor in microorganisms. As the first step, a strain of Streptomyces fradiae was selected as a producer of extracellular proteinase inhibitor. The proteinase inhibitor was purified from culture broth through ultrafiltration, gel-filtration and ion-exchange chromatography. Molecular weight of the proteinase inhibitor was estimated to be 16, 800 by SDS polyacrylamide gel electrophoresis. It was found that the proteinase inhibitor inhibited only alkaline serine proteinases such as subtilisin, $\alpha$-chymotrypsin and Promase E but not trypsin and other proteinases. The mode of inhibition against Pronase E with succinyl-phenylalanine-p-nitroanilide as a substrate was competitive.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.2
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• pp.236-241
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• 1997

Inhibitory effects of several edible plant extracts against 3-hydroxy-3-methylglutaryl coenzyme A(HMG-CoA) reductase, a rate-limiting enzyme in the biosynthesis of cholesterol, were screened. Inhibition rates of $10{\sim}15%$ were observed with hot water extracts of Allium fistulosum, Allium sativum and Cucurbita maxima. Methanol extracts of Aster scaber, Allium sativum, Zingiber officinale, Oenanthe javanica and Angelica keiskei effectively reduced the enzyme activity with inhibition rates of $29{\sim}51%$. The methanol extract of Angelica keiskei was fractionated sequentially with chloroform, ethyl acetate and n-butanol. Of the fractions ethyl acetate fraction showed the highest inhibition against the enzyme. $Luteolin-7-O-{\beta}-D-glucoside$ and hyperoside isolated from the ethyl acetate fraction of Angelica keiskei inhibited the enzyme activity by 65.5% and 14.8%, respectively, at the concentration of $30{\mu}M$.

• Applied Biological Chemistry
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• v.48 no.1
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• pp.103-108
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• 2005

${\alpha}-Amylase$ inhibitor is used to control blood glucose level by inhibiting starch digestion in the small intestine and delaying the absorption of glucose. In this study, we investigated the effect of the ethanol extracts from more than 1400 species of plants against ${\alpha}-amylase$ with the aim of developing a new ${\alpha}-amylase$ inhibitor. In the results, Cornus walteri extracts showed the highest inhibition activity. The inhibitory effect of Cornus walteri extract on the carbohydrate hydrolysis enzymes has different sensitivities against ${\alpha}-amylase$ from salivary and pancreatin and against ${\alpha}-glucosidase$ from yeast and porcine small intestine. In the study of inhibition kinetics of ${\alpha}-amylase$ and ${\alpha}-glucosidase$, Cornus walteri extract showed competitive inhibition against salivary and pancreatin while showing the combination of uncompetitive and noncompetitive inhibition against ${\alpha}-glucosidase$. The Cornus walteri extract was stable at acidic and thermal conditions. As for the blood glucose and body weight levels of Cornus walteri extract, we confirmed anti-hyperglycemic and anti-obesity effects. Also, in the investigation of the mRNA lever, Cornus walteri extract upregulated the level of GLUT4 mRNA in the quadriceps muscle.

• Microbiology and Biotechnology Letters
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• v.15 no.2
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• pp.129-134
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• 1987

Aspergillus sp. (MK-24) producing a biological active substance that inhibited the venom proteinase activity was isolated from soil. The substance also inhibited the activity of trypsin and coagulation of blood, but did not inhibit papain, $\alpha$-chymotrypsin and pepsin. The substance was partially purified from culture filtrate by precipitaion with acetone, and by chromatography of DEAE-Sepadex A-50 column and Amberlite IRC-50 ion exchange. The inhibitory substance was stable in the wide pH range from 2.0 to 12.0 at 37$^{\circ}C$, but not stable at $65^{\circ}C$ in the alkaline pH. Only 12% of the activity was decreased by the heat treatment at 10$0^{\circ}C$ for two hours. The inhibition on venom proteinase (Agkistrodon bromohoffi brevicaudus) was a mixed type. The inhibitory activity depended on the preincubation time and completely depressed by cupric, zinc and cobalt ions. The inhibition on the venom proteinase was appeared strongly on casein but not on ovalbumin or hemoglobin as a substrate.