• Korean journal of food and cookery science
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• v.26 no.2
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• pp.214-219
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• 2010

In this study, phytoestrogen for the industrial production of soybean probiotics by lactic acid bacteria (LAB) was studied in a soybean extract. Soybean was fermented with LAB, Lactobacillus plantarum KCTC 3108 and Bifidobacterum longum ATCC 15707. The change in the content of various isoflavones (aglycone and glucoside) and the $\beta$-glucosidase activity in soybean during fermentation were investigated and shown to be dependent on the starter organism. Soybean extract powder fermented with L. plantarum showed the highest $\beta$-glucosidase activity and the greatest increase in the aglycone content. After 48h of fermentation, the contents of daidzin, genistin and glycitin in L. plantarum decreased from a mean initial levels of $83.03{\pm}2.17$, $168.13{\pm}8.17$ and $20.02{\pm}1.07$, respectively, to mean levels of $5.34{\pm}3.24$, $3.79{\pm}0.57$ and $1.87{\pm}1.09\;mg$/100 g. Whereas, after 48h fermentation, the contents of daidzein, genistein and glycitein increased from a mean initial levels of $8.09{\pm}0.78$, $11.20{\pm}0.84$ and $4.71{\pm}0.46$, respectively, to mean levels of $85.76{\pm}0.84$, $175.87{\pm}2.21$ and $22.41{\pm}0.91\;mg$/100 g. Taken together, these results suggested an increase of aglycones and decrease of glucoside in isoflavones occurred during fermentation, which coincided with an increase of $\beta$-glucosidase activity in the fermented soybean extract powder.

• Korean Journal of Medicinal Crop Science
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• v.16 no.2
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• pp.74-78
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• 2008

Liquiritin in licorice (Glycyrrhiza uralensis Fisch) extract was treated with three different plant crude enzymes (Prunus dulcis enzyme; PDE, P. armeniaca enzyme; PAE and P. persica enzyme; PPE) for biotransformation. The resulting product of liquiritin was analyzed by TLC and HPLC. The ${\beta}glucosidase$ activities of crude enzymes were 259.6 U/g (PDE), 407.6 U/g (PAE) and 445.8 U/g (PPE), respectively. The liquiritin was converted to liquiritigenin after 12 hours of incubation with the crude enzymes. Liquiritigenin content reached its maximum level after the treatment with PPE at $37^{\circ}C$.

• Korean Journal of Microbiology
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• v.31 no.1
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• pp.93-98
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• 1993

To investigate the organic matter transformation in aquatic environment, seasonal fluctuations of heterotrophic activity and microbia] extracellular enzyme activity were studied in Paldang Lake, Korea. The turnover time in the water column and the sediment at the station I fluctuated between 3 -I ,300 hrs and 17-170 hrs for glucose, 5 -1.900 hrs and 15-240 hrs for protein hydrolysate and 4-350 hrs and 15-230 hrs for acetic acid, respectively, indicating that the seasonal turnover time of organic substrates fluctuated drastically. The respiration ratios of glucose. protein hydrolysate and acetate were 23-32%, 38-41% and 22-28% in the water column and 34%, 61% and 41% in the sediment. respectively. These results showed that the respiration ratios in the sediment were higher than those in the water column regardless of kinds of organic substrates. The bacterial extracellular enzyme activities of $\alpha$-glucosidase. $\beta$-glucosidase, N-acetyl-$\beta$-D-glucosaminidase and aminopeptidase were 32-44%. 31-32%, 18-34% and 61-67% in the water column, and 34%. 40%, 23% and 65% in the sediment. respectively.

• Journal of Ginseng Research
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• v.36 no.4
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• pp.418-424
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• 2012

This study focused on the enzymatic biotransformation of the major ginsenoside Rb1 into Rd for the mass production of minor ginsenosides using a novel recombinant ${\beta}$-glucosidase from Flavobacterium johnsoniae. The gene (bglF3) consisting of 2,235 bp (744 amino acid residues) was cloned and the recombinant enzyme overexpressed in Escherichia coli BL21(DE3) was characterized. This enzyme could transform ginsenoside Rb1 and gypenoside XVII to the ginsenosides Rd and F2, respectively. The glutathione S-transferase (GST) fused BglF3 was purified with GST-bind agarose resin and characterized. The kinetic parameters for ${\beta}$-glucosidase had apparent $K_m$ values of $0.91{\pm}0.02$ and $2.84{\pm}0.05$ mM and $V_{max}$ values of $5.75{\pm}0.12$ and $0.71{\pm}0.01{\mu}mol{\cdot}min^{-1}{\cdot}mg$ of $protein^{-1}$ against p-nitrophenyl-${\beta}$-D-glucopyranoside and Rb1, respectively. At optimal conditions of pH 6.0 and $37^{\circ}C$, BglF3 could only hydrolyze the outer glucose moiety of ginsenoside Rb1 and gypenoside XVII at the C-20 position of aglycon into ginsenosides Rd and F2, respectively. These results indicate that the recombinant BglF3 could be useful for the mass production of ginsenosides Rd and F2 in the pharmaceutical or cosmetic industry.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.488-492
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• 1998

This study was performed to investigate the influcence of various dietary fiber sources in Korea for activities of bacterial enzymes (${\beta}$-glucosidase, ${\beta}$-glucuronidase) and amounts of putrefactive product (indole) in aged rats. ${\beta}$-Glucosidase activity in the intestinal content was significantly lower in the seamustard 15% group than in other groups whereas the activity of ${\beta}$-glucuronidase was higher in the mugwort 15% group than other experimental groups. The amount of indole and pH in the intestinal content of aged rats were significantly lower in mugwort groups than in other groups.

• Korean Journal of Pharmacognosy
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• v.38 no.4
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• pp.358-362
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• 2007

From the EtOAc fraction of the MeOH extract of Ulmus davidiana, (-)-catechin (1), (-)-catechin-7-O-${\beta}$-D-apiofuranoside (2), and (-)-catechin-7-O-${\beta}$-D-xylopyranoside (3) were isolated and characterized on the basis of $^1H-and\;^{13}C-NMR$, and FABMS spectral data. Compounds 1-3 showed more strong reducing power activities than ${\alpha}-tocopherol$, a positive control.

• Journal of Microbiology and Biotechnology
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• v.11 no.2
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• pp.229-233
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• 2001

Trichoderma reesei Rut C-30 produced high levels of ${\beta}$-glucosidase, endo-${\beta}$-glucosidase, endo-${\beta}$-1,4-glucanase, and exo-${\beta}$-1,4-glucanase. In pilot-scale production (50-1 fermentor), productivity and yield of CMCase (carborymethyl cellulose) and FPase (filter paper activity) were 273 U/ml and 35 U/ml, and 162 FPU/l.h and 437 FPU/g, respectively. The fed-batch techniques were used to improve enzyme activities with constant cell concentration. The acidity was an important parameter and controlled at pH 3.9 and 5.0 by automatic addition of ammonium hydroxide. Cellulase powder was prepared by ammonium sulfate precipitation and its CMCase and FPase activities were 3,631 U/g and 407 U/g, respectively.

• Korean Journal of Microbiology
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• v.40 no.3
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• pp.230-231
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• 2004

The mycelia of Sparassis crispa DSMZ 5201 were cultivated at $24^{\circ}C$ for 15 days in yeast-malt extract-glucose broth (pH 4.0) and the filtrate was used as crude enzyme solution to determined the extracellular enzyme activity. The specific activity of $\alpha$-amylase was 44.27 unit/protein. The specific activities of protease, CMCase, $\beta$-glucosidase, chitinase, exo-$\beta$-l,4-glucanase were relatively high. However, a very little activity of xylanase was found.

• YAKHAK HOEJI
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• v.40 no.3
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• pp.335-339
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• 1996

Optimal medium for growth and glycosidases production of Bacteroides JY-6, an human intestinal bacterium, was general anaerobic medium or tryptic soy broth containing sod ium thioglycolate and ascorbic acid. By cocultivation of Staphylococcus R-48, Bacteroides JY-6 could be cultured in LB broth unable to culture JY-6. Heated Staphylococcus R-48 was also the inducer of the production of Bacteroides JY-6 glycosidases. These glycosidases were induced well by natural flavonoid glycosides, such as poncirin, naringin and rutin, but were not by synthetic substrates, p-nitrophenyl ${\beta$-D-glucopyranoside and p-nitrophenyl ${\alpha}$-L-rhanmopyranoside.

• Journal of Plant Biology
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• v.27 no.2
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• pp.43-50
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• 1984

Effects of IAA on the elongation and cell wall hlysocidase activities were investigated in excised rape (Brassica napus L. cv. Yongdang) hypocotyl segments. IAA promoted the elongation of rape hypocotyl segments. In rape hypocotyls, the first 10-mm segments from the hook exhibited maximal elongation and the capacity of elongation was gradually decreased with increasing distance of each 10-mm from the hook. A good correlation has been obtained between the magnitude of endogenous growth and the activities of $\alpha$, $\beta$-glucosidase and $\alpha$, $\beta$-galactosidase. However, exogenous application of IAA did not seem to enhance the tissue with IAA resulted in acidification of the incubation medium. From these data, we can conclude that IAA seems to enhance elongation of the tissue segments, at least in part, by releasing hydrogen ion into cell wall, some of which may participate in the cell wall extension process, but does not seem to trigger the activation of $\alpha$, $\beta$-glucosidase and $\alpha$, $\beta$-galactosidase.