• Food Engineering Progress
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• v.14 no.3
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• pp.243-248
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• 2010

The ${\beta}$-glucosidase (E.C. 3.2.1.21) production capabilities of lactic acid bacteria isolated from a variety of kimchi (fermented vegetables) were examined. When grown in a medium containing cellobiose as carbon source, most lactic acid bacteria showed significantly higher intracellular levels of ${\beta}$-glucosidase than the extracellular levels. A maximum intracellular ${\beta}$-glucosidase activity of 3.7${\pm}$0.5 (unit/mg protein) was obtained in the case of Weissella cibaria KFRI88010 isolated from kimchi. The optimum reaction conditions for W. cibaria KFRI88010 ${\beta}$-glucosidase activity were pH 5.0 and ${37^{\circ}C}$, and addition of divalent cations to the reaction mixture resulted in a notable decrease in enzyme activity. The ${\beta}$-glucosidase activity was enhanced twofold when W. cibaria KFRI88010 was grown in a medium containing fructose as compared with to a medium containing glucose or cellobiose.

• KSBB Journal
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• v.15 no.1
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• pp.9-13
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• 2000

In order to determine the characteristics of $\beta$-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures trom 55 to $70^{\circ}C$ and its optimum temperature was $65^{\circ}C$. The $\beta$-glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of $\beta$-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at $55^{\circ}C$ for 60 min, more than 90% of the enzyme activity was still sustained. Iron($Fe^{++}$) stimulated enzyme activity, whereas mercury($Hg^{++}$) and copper($Cu^{++}$) inhibited. Compared to salicin as a substrate, the relative activity for cellobiose was observed to be 48.6%. The apparent $K_m$ and $V_{max}$ of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.

• Korean Journal of Environmental Biology
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• v.17 no.4
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• pp.493-498
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• 1999

To verify the usefulness of enzyme activities as a index for the stability or maturity of organic refuse composting such as grape pomace, Vmax of $\beta$-glucosidase, cellobiohydrolase and alkaline phosphatase were measured. The peak values of all measured enzymes at the initial stage of composting were probably associated with easily degradable organic matter in the grape pomace and decreased gradually. But the activities of $\beta$-glucosidase and cellobiohydrolase were increased again rapidly whereas that of alkaline phosphatase remained approximately constant after 60 composting days. These results suggest that the increase of enzyme activities during the later periods of grape pomace composting process could be used as a index for their stability.

• Microbiology and Biotechnology Letters
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• v.37 no.2
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• pp.99-104
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• 2009

The $\beta$-glucosidase gene from Streptomyces coelicolor A3(2) was cloned and expressed in Escherichia coli. The ORF consisted of 1377 nucleotides encoding 51 kDa in a predicted molecular weight. Effects of pH indicated that the $\beta$-glucosidase showed similar activity using $\alpha$-pNPG($\rho$-nitrophenyl-$\alpha$-D-glucopyranoside), $\beta$-pNPG($\rho$-nitrophenyl-$\beta$-D-glucopyranoside), and $\beta$-pNPF($\rho$-nitrophenyl-$\beta$-D-fucopyranoside) at range of pH 3 to 10, and high activity using $\beta$-pNPGA ($\rho$-nitrophenyl-$\beta$-D-galactopyranoside) from pH 5 to 10, especially, 3.3 times higher activity at pH 9. Effects of temperature indicated that the $\beta$-glucosidase showed low activity using $\alpha$-pNPG, $\beta$-pNPG, and $\beta$-pNPF from $20^{\circ}C$ to $70^{\circ}C$, and increased activity using $\beta$-pNPGA from $30^{\circ}C$ to $50^{\circ}C$, 1.8 times higher activity at $50^{\circ}C$ than at $30^{\circ}C$. According to activity determination of other substrates, the enzyme was active on daidzin, genistin, and glycitin, inactive on esculin and apigenin-7-glucose. The EDTA and DTT as reducing agents inhibited $\beta$-glucosidase activity, but SDS and mercaptoethanol did not inhibit. Monovalent or divalent metal ions such as $MnSO_4$, $CaCl_2$, KCl, and $MgSO_4$ did not inhibited $\beta$-glucosidase activity. $CuSO_4$ and NaCl showed low inhibition, and $ZnSO_4$ inhibited 3.3 times higher than control.

• KSBB Journal
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• v.5 no.2
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• pp.141-149
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• 1990

$\beta$-glucosidase derived from Aspergillus niger was immobilized by (1) covalent linkage on chitin and chitosan with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA93 after succinylation, and (3) entrapment on alginate and polyacrylamide gels with various cross linking agents. The retention yield of $\beta$-glucosidase immobilized on chitosan was 31.5% and operational stability was 69% after continuous operation at column reactor(5$0^{\circ}C$ at pH 4.8) for 15 days. The retention yield and operational stability were 24.7% and 60% respectively, in adsorption on Amberite IRA 93. On the other hand, the entrapment method by alginate and polyacrylamide gel was identified to be not appropriate due to the continuous elution of inlmobilized $\beta$-glucosidase. Optimum conditions for the immobilization on chitosan were also studied with optimum pH of 4.8 and glutaraldehyde concentration of 0.4%(w/v). The properties and stability of immobilized $\beta$-glucosidase are also investigted. The conversion yield of cellobiose to glucose was also analyzed using the column type enzyme reactor to evaluate the effectiveness of immobilized enzyme.

• The Journal of Natural Sciences
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• v.8 no.2
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• pp.57-61
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• 1996

The $\beta$-glucosidase enzyme was purified from E. coli carrying Cellulomonas fimi $\beta$-glucosidase gene. SDS-PAGE and analytical gel filtration revealed that molecular weight of this enzyme was 56,000 dalton and consisted of a single polypeptide.Inhibition caused by heavy metals and activation by dithiothreitol suggest the existence of essential thiol group in the enzyme. The enzyme was not active on maltose (glucose $\alpha$-1,4-glucose) which has a $\alpha$-linkage, whereas it was active on lactose (glucose $\beta$-1,4-glucose), PNPG (p-nitrophenyl $\beta$-D-glucopyranoside) and PNPC (p-nitrophenyl $\beta$-D-cellobioside), although its reaction rates were different.

• Journal of the Korean Wood Science and Technology
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• v.38 no.3
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• pp.251-261
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• 2010

Cellulase from Formiptosis pinicola KMJ812 is an efficient cellulose degradation enzyme complex, especially with a high ${\beta}$-glucosidase activity. In this study, the change in enzymatic characteristics by immobilization and the reduction of immobilized enzyme activity by repeated usages were evaluated using cellulases from F. pinicola KMJ812. Among tested four resins, Duolite A568 resin had the best enzyme activity yield with 61.7% cellulase activity and 64.4% ${\beta}$- glucosidase activity during the cellulase immobilization. The best reaction temperature was $55^{\circ}C$ for both cellulase and ${\beta}$-glucosidase activities which were higher than the unimmobilized soluble cellulases. The best reaction pH was 4.0 for cellulase activity which was a little more basic than a soluble form and 4.5 for ${\beta}$-glucosidase activity. The immobilized cellulase activity was remained 98% of the beginning activity after 72 h incubation at $50^{\circ}C$ and 50% of the beginning activity after eight times usage at $50^{\circ}C$.

• The Korean Journal of Zoology
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• v.32 no.3
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• pp.290-303
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• 1989

The activities of $\beta$-glucosidase, $\beta$-glucuronidase and N-acetyl-$\beta$-glucosaminidase were measured to investigate the relationships of them to sexual maturity. Peritoneal injections of testosterone and dibutyryl cAMP to rats were carried out. As a result, the activities of $\beta$-glucosidase and N-acetyl-$\beta$-glucosaminidase were significantly decreased from the third day and that of P -glucurondiase on the seventh day in the castrated groups. In addition, ihe activities of these three enzymes were significantly increased in the testosterone treated groups for 7 days. In case of dbcAMP injection, the activities of these three enzymes were similar to those of castrated groups or had a tendency to be decreased. On electron microscopic examination, principal cells, basal cells and narrow cells were observed in all regions of epididymis. Principal cells were general forms of columnar epithelial cells. Narrow cells had a number of small vesicles and light cells showed low electron density in comparison to other epithelial cells in cauda epididymis. Halo cells were migrating leucocytes btween epithelial cells.

• 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.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.