• Archives of Pharmacal Research
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• v.21 no.1
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• pp.17-23
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• 1998

Flavonoid glycosides were metabolized to phenolic acids via aglycones by human intestinal microflora producing ${\alpha}$-rhamnosidase, exo-${\beta}$-glucosidase, endo- ${\beta}$-glucosidase and/or ${\beta}$-glucuronidase. Rutin, hesperidin, naringin and poncirin were transformed to their aglycones by the bacteria producing ${\alpha}$-rhamnosidase and ${\beta}$-glucosidase or endo- ${\beta}$-glucosidase, and baicatin, puerarin and daidzin were transformed to their aglycones by the bacteria producing ${\beta}$glucuronidase, C-glycosidase and ${\beta}$-glycosidase, respectively. Anti-platelet activity and cytotoxicity of the metabolites of flavonoid glycosides by human intestinal bacteria were more effective than those of the parental compounds. 3,4-Dihydroxyphenylacetic acid and 4-hydroxyl-phenylacetic acid were more effective than rutin and quercetin on anti-platelet aggregation activity. 2,4,6-Trihydroxybenzaidehyde, quercetin and ponciretin were more effective than rutin and ponciretin on the cytotoxicity for tumor cell lines. We insist that these flavonoid glycosides should be natural prodrugs.

• Korean Journal of Food Science and Technology
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• v.25 no.2
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• pp.191-195
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• 1993

The intestinal microflora of humans is an extraordinarily complex mixture of microorganisms, the majority of which are anaerobic bacteria. Amongst them, most prevalent bacteria are Bacteroides, Eubacterium, Peptococcus, Bifidobacteria. We isolated a Bacteroides fragilis strain from a Korean adult and examined various glycosidase activities of this strain. The activities of $N-acetyl-{\beta}-glucosaminidase,\;{\alpha}-fucosidase$, ${\beta}-glucuronidase$, chitobiase and PNPCase were stronger in Bacteroides fragilis Roid 8 than in other intestinal anaerobic bacteria. $N-acetyl-{\beta}-glucosaminidase$ was strongest, followed by ${\alpha}-fucosidase$, ${\beta}-glucuronidase$ and PNPCase. The activities of ${\beta}-galactosidase$, ${\beta}-xylosidase,\;{\alpha}-arabinofuranosidase$ were not present or very low. The activities of ${\alpha}-glucosidase$, ${\beta}-glucosidase$ and ${\alpha}-galactosidase$ were present but at a lower level than in Bifidobacterium. The effect of the carbon sources on the production of $N-acetyl-{\beta}-glucosaminidase$, ${\alpha}-fucosidase$, ${\beta}-glucuronidase$ and PNPCase of Bacteroides fragilis Roid 8 was investigated. :.actose and glucose lowered the production of the varous glycosidase enzymes studied in this work. In addition, we investigated the optimum temperature and pH of each glycosidase from Bacteroides fragilis Roid-8 using crude enzyme preparations.

• The Korean Journal of Food And Nutrition
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• v.14 no.6
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• pp.591-595
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• 2001

The antioxidant and synergistic effects of sesame oil cake extract treated with $\beta$ -glucosidase were examined. The sesamin and sesamolin were identified from the 80% ethanol extract of seame oil cake treated with $\beta$ -glucosidase, which suggested the presence of the active substances as their glycosides in sesame seed. The contents of sesamin and sesamolin in sesame oil cake extract were about 8.32% (8,315.4 mg/100g) and 0.28% (2,824.5mg/100g) , respectively. Sesame oil cake extract showed antioxidant activity at concentrations of 50ppm, 100ppm and 200ppm, and the effect was Increased with the addition of sesame oil cake extract. The antioxidant effect of sesame oil cake extract was stronger than that of $\alpha$-tocopherol or ascorbyl palmitate, but weaker than of BHT Also, when the sesame oil cake extract(50ppm) was used in combination with $\alpha$-tocopherol(50 ppm), the sesame oil cake showed very strong synergistic effect.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.30 no.3 s.47
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• pp.415-418
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• 2004

Arbutin is a glycosylated hydroquinone found at high concentration in certain plants capable of surviving extreme and sustained dehydration. It has been reported to have an inhibitory effect of melanogenesis and to be hydrolyzed easily to yield glucose and hydroquinone by ${\beta}-glucosidase.$ While hydroquinone also has an anti-melanogenic effect, however, is carefully used as a topical whitening agent because of side effects. The present study was undertaken to examine the inhibitory effect of an whitening agent containing arbutin and ${\beta}-glucosidase$ on UV radiation induced pigmentation in human skin. Experimental subjects were UVB-irradiated on the back. UVB-irradiated areas were assigned to three groups: arbutin and ${\beta}-glucosidase$ treated group, vehicle control, and no-application control. Arbutin and ${\beta}-glucosidase$ treatment inhibited pigmentation by 50.17 percent, compared with the controls (N : 10: P<0.05). These results suggest that the whitening agent containing arbutin and ${\beta}-glucosidase$may be used as an agent to inhibit melanin formation induced by UV radiation.

• Applied Biological Chemistry
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• v.38 no.6
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• pp.490-495
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• 1995

Among the cellulases by Cellulomonas sp. KL-6. CMCase and filter paperase, which were produced as the out enzymes of cell, had been much produced, but very small amounts of ${\beta}-glucosidase $, the enzyme of which is cell bound form, was produced by this organism. The optimal culture times for CMCase and filter paperase productions were 5 days, while that of ${\beta}-glucosidase$ was 4 days. When this strain was cultured under the optimal medium for enzyme production, CMCase, FPase and ${\beta}-glucosidase$ were $82\;units/m{\ell},\;80\;units/m{\ell}\;and\;1.2\;units/m{\ell}$, respectively. Thus these results were showed to increase enzyme productivities as about $60{\sim}70%$ than those produced in basal medium. $CaCO_3$ injected to the medium as the ratio of 0.1% was not only enhanced cellulase activities but also effective as acid neutralizing agent. The production effects of lignase and lactase by this bacterium in filter paper medium was not appeared.

• Korean Journal of Agricultural Science
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• v.3 no.2
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• pp.225-234
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• 1976

To elucidate ${\beta}$-glucosidase formation on various carbon scurces by cellulolytic bact-eia, Cellulomonas sp. CS1-1, the strain was grown on Nutrient Yeast Broth, carboxymethyl cellulose, avicel and cellobiose using a Ouickfit FVIL fermentor operated in batch, and the growth characteristics on those substrates and ${\beta}$-glucosidase distribution of extra and intracellular enzyme components were studied. The results were: 1) ${\beta}$-glucosidase was always intracellular, and was formed under all growth conditions tested, ii) but levels of relative activities were higher when the culture was grown on cellobiose and on avicel, iii) the relative activities were always maximum during the growth phase of the organism irrespective of the substrate used.

• Korean Journal of Food Science and Technology
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• v.38 no.4
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• pp.461-468
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• 2006

콩가루 50, 75, 100% 첨가 콩 반죽에 0, 1, 3%의 아몬드 첨가와 0, 20, 40분의 반죽 정치시간을 통해 제조 된 콩 과자 반죽에서 ${\beta}-glucosidase$ 활성을 측정하였고 콩 과자에서의 이소플라본 함량 및 aglycone 이소플라본 변화를 연구하였다. 일반적으로 콩가루 첨가량이 증가 될수록, 아몬드 첨가량이 증가할수록 반죽의 ${\beta}-glucosidase$ 효소 활성도는 높았으며 반죽 정치시간 20분이 0분이나 40분 보다 효소 활성이 유의적으로 높았다. 콩 과자 반죽에 포함된 이소플라본 함량은 예상된 함량 보다 약 15.2-31.5% 가량 적게 검출 되었다. 콩가루의 이소플라본 분포에 비해 콩 과자는 aglycones과 $6@-O-{\beta}-glucosides$는 증가하였고 $6@-O-malonyl-{\beta}-glucosides$는 감소하였다. 콩 과자의 aglycone 함량 증가에는 아몬드 첨가 보다 반죽 정치시간 증가가 더 효율적이었다.

• Journal of Microbiology and Biotechnology
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• v.1 no.3
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• pp.188-196
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• 1991

The ${\beta}-glucosidase$ was purified to homogeneity from the culture filtrate of P. verruculosum by column chromatography. The enzyme was a glycoprotein with a relative size of approximately 220 kDa with an isoelectric point of 4.8, which was composed of dimeric protein of 105 kDa. The enzyme was stable up to $60^{\circ}C$ and the presence of glycerol significantly increased its thermostability. The enzyme was found to hydrolyze both ${\beta}-aryl$ and ${\beta}-alkyl-glucosides$ in addition to ${\beta}-glucosyl$ glucose and catalyzed glucosyl transfer to cellobiose. The enzyme attacked laminarin in an exotype-like fashion. The apparent Km's of the enzyme toward cellobiose, laminaribiose, laminarin were 0.53 mM, 0.35 mM and 1.11 mM, respectively. Glucose and glucono-${\delta}-lactone$ were competitive inhibitors for the enzyme. Copper ($Cu^{2+}$), mercury ($Hg^{2+}$) and p-chloromercuribenzoate were strong inhibitors of the enzyme. The immunoblotting result revealed that one form of ${\beta}-glucosidase$ was biosynthesized, irrespective of carbon sources used. Polyacrylamide gel electrophoresis analysis of the in vitro translated product of total RNA from avicel grown mycelium established that the P. verruculosum ${\beta}-glucosidase$ precursor was approximately 95 kDa in size. The amino acid composition and N-terminal amino acid sequence are given.

• Journal of Life Science
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• v.21 no.11
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• pp.1579-1585
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• 2011

Natural anti-diabetic semipurified ethyl acetate fraction was isolated from the submerged-liquid culture of Agaricus blaze Murill (AB) in a medium containing soybean flakes. Hot-water extract of AB (HEAB) was prepared by extraction at $121^{\circ}C$ for 60 min, followed by filtering through a filter presser filled with diatomate. The ${\beta}$-glucan-free HEAB, which was a supernatant fraction from HEAB by precipitation in an 80% ethanol solution, was fractionated into hexane, chloroform, ethyl acetate, and butanol fractions. The inhibition of the ${\alpha}$-glucosidase activity by fractions was 59.0, 17.0, 61.6, and 37.9%, respectively, suggesting that ethyl acetate fraction was the most active. A subfraction having a strong ${\alpha}$-glucosidase inhibitory activity (80.4%) was isolated from the ethyl acetate fraction. This subfraction contained isoflavones (genistin and daidzin) and their conjugates with sugars as potent inhibiters of ${\alpha}$-glucosidase activity. These results suggest that the ethyl acetate fraction or HEAB containing isoflavones and their sugars conjugates could be useful sources for controlling blood sugar levels in humans.

• Microbiology and Biotechnology Letters
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• v.18 no.1
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• pp.39-43
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• 1990

The inhibitor had the inhibitory activities against hydrolysis of PNPG, sucrose and ONPG by $\alpha$-Dglucosidase, $\alpha$ - and $\beta$ -galactosidase, but it did not inhibit amylases and other carbohydrases. Kinetic studies exhibited that the inhibitory substance non-competitively inhibited the enzyme reaction with a Ki value of 118 $\mu$g/m$\ell$, and enzyme-inhibitor complex was formed slowly.