• Korean Journal Plant Pathology
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• v.13 no.4
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• pp.225-231
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• 1997

Activities of polygalacturonase, laccase, and intra- and extra-cellular $\beta$-glucosidase produced by 20 Botrytis cinerea isolates in liquid culture media containing cucumber cell was as a carbon source were measured and their relationships to the pathogenicity were analyzed. No significant correlations between these enzyme activities and the pathogenicity of B. cinerea were found. Mycelial growth rate on Bayendamm media, however, was higthly correlated with the pathogenicity (r=0.522) anong these isolates. Immuno-blot analysis of the culture filtrate using antibody against against exo-polygalacturonase revealed that only one band with molecular weight of 66 kDa was detected amone 34 tested isolates. It appears that these enzymes may not be primary factors in dermining the pathogenicity of B. cinerea.

• Korean Journal of Microbiology
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• v.35 no.2
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• pp.128-132
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• 1999

The effects of diet on the composition of fecal microflora in mouse and the aclivilies of several enzymes in the leces were investigated. Vegetarian dietary groups were found to contain about ten lines higher numbers of Locmbocillus and B$&bacterizml than animal dietary groups. An~rnal dietmy groups were found to contain about 5 tolo times higher numbers of anaerobic Closhidia and Bocieriocles than the vegeterian detary groups. Fccal microbial $\beta$-glucosidase, $\beta$-glucm'onidase, ii-yptophanase and orease activilies in ihe animal dietary groups were shown lo be 30 to 50% hgher than those in h e vegetarian detary groups.

• Journal of Microbiology and Biotechnology
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• v.17 no.6
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• pp.905-912
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• 2007

A novel ${\beta}-glucosidase$ gene, bglA, was isolated from uncultured soil bacteria and characterized. Using genomic libraries constructed from soil DNA, a gene encoding a protein that hydrolyzes a fluorogenic analog of cellulose, 4-methylumbelliferyl ${\beta}-D-cellobioside$ (MUC), was isolated using a microtiter plate assay. The gene, bglA, was sequenced using a shotgun approach, and expressed in E. coli. The deduced 55-kDa amino acid sequence for bglA showed a 56% identity with the family 1 glycosyl hydrolase Chloroflexus aurantiacus. BglA included two conserved family 1 glycosyl hydrolase regions. When using $p-nitrophenyl-{\beta}-D-glucoside$ (pNPG) as the substrate, the maximum activity of the purified ${\beta}-glucosidase$ exhibited at pH 6.5 and $55^{\circ}C$, and was enhanced in the presence of $Mn^{2+}$. The $K_m\;and\;V_{max}$ values for the purified enzyme with pNPG were 0.16 mM and $19.10{\mu}mol/min$, respectively. The purified BglA enzyme hydrolyzed both pNPG and $p-nitrophenyl-{\beta}-D-fucoside$. The enzyme also exhibited substantial glycosyl hydrolase activities with natural glycosyl substrates, such as sophorose, cellobiose, cellotriose, cellotetraose, and cellopentaose, yet low hydrolytic activities with gentiobiose, salicin, and arbutin. Moreover, BglA was able to convert the major ginsenoside $Rb_1$ into the pharmaceutically active minor ginsenoside Rd within 24 h.

• Korean journal of food and cookery science
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• v.17 no.3
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• pp.211-217
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• 2001

The objective of this study was to evaluate the effect of functional herbal foods on the growth of intestinal lactic acid bacteria. When Bifidobacterium breve and human intestinal microflora were inoculated in the general anaerobic medium which contained each functional food water extract, most of functional herbal foods induced the growth of lactic acid bacteria by decreasing pH of the broth. The pH decreasing effects of Liriipe platyphylla and Platycodon grandiflorum were excellent. The growth of lactic acid bacteria effectively inhibited the bacterial enzymes, $\beta$-glucosidase and $\beta$ -glucuronidase. Eugenia caryophyllata and Liriipe platyphylla potently inhibited the productivity of P -glucosidase of B. breve and human intestinal bacteria. Cinnamomum cassia, Gardenia jasminoides and Platycodon grandiflorum potently inhibited the productivity of $\beta$-glucuronidase of human intestinal bacteria. The growth component isolated from Platycodon grandiflorum was sucrose (compound B).

• Journal of Applied Biological Chemistry
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• v.49 no.4
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• pp.162-164
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• 2006

The roots of Codonopsis lanceolata afforded tangshenoside I(1) and $\beta$-adenosine (2) as $\alpha$-glucosidase inhibitors. Their structures were unambiguously determined by 1D and 2D NMR data including HMQC and HMBC experiments. Compounds 1 and 2 exhibited weak $\alpha$-glucosidase inhibitory activities in vitro with $IC_{50}$ of 1.4 and 9.3 mM, respectively.

• Microbiology and Biotechnology Letters
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• v.25 no.1
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• pp.44-50
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• 1997

$\beta $-Glucosidase (EC 3.2.1.21) was purified from Aspergillus niger SFN-416 by a sequential process of ammonium sulfate precipitation, Sepadex G-100 and DEAE-Sephacel column chromatography. Molecular weight of the enzyme was 46, 000 daltons. The K$_{m}$ and V$_{max}$ values for PNPG were 0.67 mM and 25 moles/ml $\cdot $min., respectively. The optimum pH and temperature of the enzyme activity were 3.5 and 58$\circ $C, respectively. The enzyme activity was decreased by addition of metal ions, and increased by addition of metanol, ethanol, isopropanol and 1-butanol at a concentration of 10% (v/v). Stability of the enzyme was increased by addition of isopropanol and 1-butanol at a concentration of 10% (v/v).

• Microbiology and Biotechnology Letters
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• v.14 no.5
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• pp.377-383
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• 1986

About 300 cellulolytic actinomycetes isolated from soils were tested for their cellulase activities estimated by means of filter paper swelling and carboxymethyl cellulose saccharifying activity. Then, 16 isolates which had shown relatively high levels of CMCase activity were selected and examined for their abilities of $\beta$-glucosidase production. Among them strain No. 109 was found to have highest level of intracellular $\beta$-glucosidase, and selected for the further studies. In this paper, the cultural, morphological and physiological properties, and cell wall composition of strain No. 109 were described in relation to the taxonomic status of this actinomycete. Based on the results obtained in these experiments strain No. 109 was identified to be a similar species to Streptomyces tanashiensis.

• KSBB Journal
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• v.13 no.1
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• pp.20-25
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• 1998

Optimum conditions of the cellulose-hydrolysis reaction with mixed enzymes(cellulase extracted from Penicellium funiculosum mixed with $\beta$-glucosidase extracted from Almod) were investigated to increase the production of glucose from cellulose. Experimental result showed that optimum conditions fro pH, activity ratio of $\beta$-glucosidase to cellulase, concentration of mixed enzymes, concentration of cellulose as a substrate, and temperature range were 4.2, 0.4, 0.8, U/mL, 40 g/L, and 37$\pm$3$^\circ C$, respectively. In these conditions, quantities of glucose productions by using mixed enzymes were larger than those by using cellulase at optimum conditions.

• Biomolecules & Therapeutics
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• v.6 no.4
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• pp.364-370
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• 1998

Glycosidase inhibitors from urine of Bombyx mori were isolated and their inhibitory activities on glycosidases were evaluated. Six compounds were isolated by using several ion exchange columns, and their chemical structures were identified by the physicochemical and spectral data. Compound IV, V and Ⅵ were identified as 1-deoxynojirimycin, fagomine and 1,4-dideoxy-1,4-imino-D-arabinitol, respectively. Among six compounds isolated,1-deoxynojirimycin(IV) was the most potent inhibitor on $\alpha$-glucosidase and $\beta$-galactosidase of rat intestine, and its inhibitory activities for trehalase and almond $\beta$-glucosidase were relatively weak. Compound V and Ⅵl retained a little inhibitory potency toward $\alpha$-glucosidase and $\beta$-galactosidase. Compound II and III, however, have been found to have no effect on all glycosidases tested in this study.

• Mycobiology
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• v.39 no.2
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• pp.118-120
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• 2011

The ability of Ganoderma to produce extracellular enzymes, including ${\beta}$-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. ${\beta}$-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for ${\beta}$-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neojaponicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.