• YAKHAK HOEJI
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• v.37 no.2
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• pp.187-192
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• 1993

Approximately 1% of intestinal bacteria of human and rats was alkalotolerant. Among these bacteria of human, bacteria producing $\beta$-glucosidase, $\beta$-glucuronidase and sulfotransferase were 40%, 4% and 0%, respectively. Among alkalotolerant intestinal bacteria of rats, bacteria producing, these enzymes were 70%, 8% and 0%, respectively. $\beta$-Glucosidase and $\beta$-glucuronidase of alkalotolerant intestinal bacteria of human and rat were induced by the medium of high pH: these enzymes activities were increased by elevating pH of the medium, but the growths were not changed. The enzyme activities at the medium of pH 7 were about ten-fold higher than those at the medium of pH 6.

• Food Science and Biotechnology
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• v.17 no.5
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• pp.1021-1024
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• 2008

Genistein, one of the isoflavones in doenjang, is generally known to prevent various cancers, osteoporosis, climacterium, and menopause symptoms, and has better bioavailability and healthful physiological effects than its glucoside, genistin. In both traditional and commercial doenjangs, genistein content ranged from 370 to 1,510 mg/kg, however, significant amounts of genistin also existed at the level of 190 to 350 mg/kg. After treating with corn $\beta$-glucosidase, over 84% of genistin in doenjang was converted to genistein. However, physiochemical characteristics such as pH, viscosity, 2-thiobarbituric acid (TBA) value, and color were not changed significantly after corn $\beta$-glucosidase treatments. Therefore, this study shows that the improved doenjang with the increased genistein content can be produced using corn $\beta$-glucosidase.

• Korean Journal of Food Science and Technology
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• v.44 no.3
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• pp.331-336
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• 2012

In this study, we selected Gardeniae fructus (GF) as an anti-inflammatory functional material and improved the biological activity of GF through the treatment of ${\beta}$-glucosidase. For the simple evaluation of anti-inflammatory activity, the inhibitory activity of GF extract (GFE) on the production of NO by RAW264.7 cells in the presence of LPS was examined. ${\beta}$-glucosidase originating from Aspergillus niger or Aspergillus fumigatus has effectively improved the anti-inflammatory activity of GFE. The enzyme treatment raised the activity of GFE by more than 10 times. The optimum conditions for the enzyme reaction were at pH 4.6, $45^{\circ}C$, and 20 U/mL for 24 h with agitation. In addition, in vitro production of cytokines (IL-$1{\beta}$, IL-6, TNF-${\alpha}$), COX-2, and the NF-${\kappa}B$ activation of RAW264.7 cells decreased more in the presence of GFE treated with ${\beta}$-glucosidase originating from Aspergillus niger (GFAN) than in the presence of GFE. These results suggest that enzyme-treated GFE might be a potential candidate for natural anti-inflammatory food materials.

• Journal of Microbiology and Biotechnology
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• v.8 no.5
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• pp.441-448
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• 1998

A cellobiose-utilizing recombinant yeast having $\beta$-glucosidase activity was developed for ethanol production from a mixture of glucose and cellobiose. Using $\delta$-sequences of Tyl transposon of yeast as target sites for homologous recombination, a heterologous gene of $\beta$-glucosidase was integrated into the chromosome of Saccharomyces cerevisiae. The $\delta$-integrated recombinant yeast, Saccharomyces cerevisiae L2612 (Pb-BGL), showed perfect mitotic stability even in nonselective media and showed ca. 1.5 fold higher $\beta$-glucosidase activity than the recombinant yeast harboring the $2\mu$-based plasmid vector system. A mathematical model was developed to describe the $\beta$-glucosidase formation and ethanol production from the Saccharomyces cerevisiae L2612 ($p\delta-BGL$). The model newly described that the heterologous $\beta$-glucosidase production mediated by ADH1 promoter is regulated by glucose and repressed by ethanol.

• Journal of Microbiology and Biotechnology
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• v.24 no.6
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• pp.788-794
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• 2014

An extracellular ${\beta}$-glucosidase from Aspergillus niger Au0847 was purified to homogeneity by precipitation with ammonium sulfate, anion exchange, and gel filtration. The purified protein was composed of two subunits with molecular masses of 110 and 120 kDa. Au0847 ${\beta}$-glucosidase exhibited relatively high thermostability and pH stability, and its highest activity was obtained at $65^{\circ}C$ and pH 4.6, respectively. As a potential metalloprotein, its enzymatic activity was potently stimulated by manganese ion and DTT. The ${\beta}$-glucosidase displayed avid affinity and high catalytic efficiency for geniposide. Au0847 ${\beta}$-glucosidase has potential value as an industrial enzyme for the hydrolysis of geniposide to genipin.

• Journal of the Korean Wood Science and Technology
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• v.35 no.5
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• pp.100-108
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• 2007

$\beta$-Glucosidase from Laetiporus sulphureus among the enzymes related to lignocellulosic biomass degradation to sugars for using alternative bioethanol production was characterized. The highest activity of $\beta$-glucosidase was obtained on cellobiose at shaking culture. For the characterization and purification of $\beta$-glucosidase culture solution was concentrated and then purified by FPLC using ion exchange and size exclusion column. According to the results of SDS-PAGE, native PAGE and microfluidic system of purified enzyme, protein band was observed at about 132 kDa. Optimal pH and temperature of purified $\beta$-glucosi-dase were 5.0 and $60^{\circ}C$, respectively. In the kinetic properties of $\beta$-glucosidase on various substrates such as sophorose, gentiobiose and cellobiose, $K_m$ was 0.81, 1.07 and 1.70 mM, respectively.

• Microbiology and Biotechnology Letters
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• v.20 no.2
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• pp.164-168
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• 1992

Enzymatic properties of avicelase, carboxymethyl cellulase (CMCase) and P-glucosidase produced by Cellulomonas sp. YE-5 were studied. Optimal temperature and pH of avicelase were 40t and 6.0, and those of CMCase and P-glucosidase were $45^{\circ}C$ and 6.5. Avicelase and CMCase were stable between pH 5.0 and 9.5, and &glucosidase was stable between pH 5.5 and 8.0. Avicelase and P-glucosidase were inactivated when incubated at $35^{\circ}C$ for 6 hrs, and CMCase was at $40^{\circ}C$ for 6 hrs. All cellulases were strongly inhibited by $Cu^{2+} \; and \; Zn^{2+}. K_m$ values of avicelase for avicel, CMCase I and CMCase II for CM-cellulose, and ($\beta$-glucosidase for p-nitrophenyl-$\beta$-D-glucoside (PNPG) were 4.76, 16.4, 16.4 $\mu g$/ml and 3.51 mM, respectively.

• Journal of Microbiology and Biotechnology
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• v.23 no.11
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• pp.1577-1585
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• 2013

Bioethanol production from lignocellulose is considered as a sustainable biofuel supply. However, the low cellulose hydrolysis efficiency limits the cellulosic ethanol production. The cellulase is strongly inhibited by the major end product cellobiose, which can be relieved by the addition of ${\beta}$-glucosidase. In this study, three ${\beta}$-glucosidases from different organisms were respectively expressed in Saccharomyces cerevisiae and the ${\beta}$-glucosidase from Saccharomycopsis fibuligera showed the best activity (5.2 U/ml). The recombinant strain with S. fibuligera ${\beta}$-glucosidase could metabolize cellobiose with a specific growth rate similar to the control strain in glucose. This recombinant strain showed higher hydrolysis efficiency in the cellulose simultaneous saccharification and fermentation, when using the Trichoderma reesei cellulase, which is short of the ${\beta}$-glucosidase activity. The final ethanol concentration was 110% (using Avicel) and 89% (using acid-pretreated corncob) higher than the control strain. These results demonstrated the effect of ${\beta}$-glucosidase secretion in the recombinant S. cerevisiae for enhancing cellulosic ethanol conversion.

• Korean Journal of Microbiology
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• v.35 no.1
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• pp.35-40
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• 1999

Effects of different molecular size fractions (100,000 nMW-0.1 $\mu\textrm{m}$m, 10,000 nMW-100,000 nMW and 1,000 nMW-'L0,000 nMW) of dissolved organic matter on the bacterial numbers and $\beta$-glucosidase activities in Lake Soyang were investigated. Even though the concentrations and characteristics of each fractions were different, bacterial growth curves of each fractioii were Lypical and similar. Each growth curve had highest peak of $1.1{\times}10^{7}$ cells $ml^{-1}$. But, the $\beta$-lucosidase activitics of each fraction were quite different. In high molecular weight fraction (HMW: 100,000 nMW-0.1 $\mu\textrm{m}$m), Vmax of Pglucosidase activity ranged from 550 to 1,160 nmol $1^{-1}$.$hi^{-1}$, but in low molecular weight f~action (1,000 nMW-10,000 nMW), that ranged from 1 to 14 om01 1$^[-1}$${-1}$

• Korean Journal of Food Science and Technology
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• v.31 no.6
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• pp.1405-1409
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• 1999

This study was conducted to investigate the isoflavone contents of soybeans, Meju, and Doenjang. $The\;{\beta}-glucosidase$ activities were also determined and characterized in soybeans, Meju, and Doenjang. The total concentration of daidzein was 406 mg/kg of soybeans, 433 mg/kg of Meju, and 538 mg/kg of Doenjang. Aglycones compose 26.03% of total isoflavones in soybeans, 61.96% in Meju, and 107.68% in Doenjang. The total concentration of genistein was 484, 200 and 538 mg/kg of soybeans, Meju and Doenjang, respectively. Aglycones compose 19.49% of total isoflavones in soybeans, 68.52% in Meju, and 85.26% in Doenjang. The ${\beta}-glucosidase$ activity was detected in soybeans (5.65 units/mg protein), Meju (2.04 units/mg protein), and Doenjang (0.69 units/mg protein). The optimal pH of ${\beta}-glucosidase$ activities were $6.5{\sim}7.0$ and the optimal temperature of ${\beta}-glucosidase$ activities was $50^{\circ}C$.