• Title/Summary/Keyword: $V_{}$ max/

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Evaluation and Verification of the Attenuation Rate of Lead Sheets by Tube Voltage for Reference to Radiation Shielding Facilities (방사선 방어시설 구축 시 활용 가능한 관전압별 납 시트 차폐율 성능평가 및 실측 검증)

  • Ki-Yoon Lee;Kyung-Hwan Jung;Dong-Hee Han;Jang-Oh Kim;Man-Seok Han;Jong-Won Gil;Cheol-Ha Baek
    • Journal of the Korean Society of Radiology
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    • v.17 no.4
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    • pp.489-495
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    • 2023
  • Radiation shielding facilities are constructed in locations where diagnostic radiation generators are installed, with the aim of preventing exposure for patients and radiation workers. The purpose of this study is seek to compare and validate the trend of attenuation thickness of lead, the primary material in these radiation shielding facilities, at different maximum tube voltages by Monte Carlo simulations and measurement. We employed the Monte Carlo N-Particle 6 simulation code. Within this simulation, we set a lead shielding arrangement, where the distance between the source and the lead sheet was set at 100 cm and the field of view was set at 10 × 10 cm2. Additionally, we varied the tube voltages to encompass 80, 100, 120, and 140 kVp. We calculated energy spectra for each respective tube voltage and applied them in the simulations. Lead thicknesses corresponding to attenuation rates of 50, 70, 90, and 95% were determined for tube voltages of 80, 100, 120, and 140 kVp. For 80 kVp, the calculated thicknesses for these attenuation rates were 0.03, 0.08, 0.21, and 0.33 mm, respectively. For 100 kVp, the values were 0.05, 0.12, 0.30, and 0.50 mm. Similarly, for 120 kVp, they were 0.06, 0.14, 0.38, and 0.56 mm. Lastly, at 140 kVp, the corresponding thicknesses were 0.08, 0.16, 0.42, and 0.61 mm. Measurements were conducted to validate the calculated lead thicknesses. The radiation generator employed was the GE Healthcare Discovery XR 656, and the dosimeter used was the IBA MagicMax. The experimental results showed that at 80 kVp, the attenuation rates for different thicknesses were 43.56, 70.33, 89.85, and 93.05%, respectively. Similarly, at 100 kVp, the rates were 52.49, 72.26, 86.31, and 92.17%. For 120 kVp, the attenuation rates were 48.26, 71.18, 87.30, and 91.56%. Lastly, at 140 kVp, they were measured 50.45, 68.75, 89.95, and 91.65%. Upon comparing the simulation and experimental results, it was confirmed that the differences between the two values were within an average of approximately 3%. These research findings serve to validate the reliability of Monte Carlo simulations and could be employed as fundamental data for future radiation shielding facility construction.

Mechanism of Erectogenic Effect of the Selective Phosphodiesterase Type 5 Inhibitor, DA-8159

  • Doh, Hyoun-Mie;Shin, Chang-Yell;Son, Mi-Won;Ko, Jun-Il;Yoo, Moo-Hi;Kim, Soon-Hoe;Kim, Won-Bae
    • Archives of Pharmacal Research
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    • v.25 no.6
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    • pp.873-878
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    • 2002
  • OA-8159, a new Phosphodiesterase (PDE) 5 inhibitor, has exhibited potent erectogenic potential in a penile erection test in rats and anesthetized dogs. In this study, we investigated the mechanism of its erectogenic activity by measuring the activity of OA-8159 against a various PDE isozymes and assessing cGMP and cAMP formation in a rabbit corpus cavernosum in vitro. DA-8159 inhibited the PDE 5 activity in rabbit and human platelets, which the $IC_{50}$ was 5.84$\pm$1.70 nM and 8.25$\pm$2.90 nM, respectively. The $IC_{50}$ of DA-8159 on PDE 1, PDE2, PDE 3 and PDE 6 were 870$\pm$57.4 nM, $101\pm$5 $\mu$M, 52.0$\pm$3.53 $\mu$M and 53.3$\pm$2.47 nM, respectively. This suggests that DA-8159 is a potent, highly selective, competitive inhibitor of PDE 5-catalyzed cGMP hydrolysis. The rates of cGMP hydrolysis catalyzed by human platelets-derived PDE 5 as a function of the cGMP concentration (5~100 nM) and two-fixed DA-8159 concentration (11.3 and 18.8 nM) were investigated in order to characterize the mode of PDE 5 inhibition by DA-8159. DA-8159 increased the apparent 4K_{m}$ value for cGMP hydrolysis but had no effect on the apparent $V_{max}$, indicating a competitive mode of inhibition. DA-8159 increased the cGMP concentrations in the rabbit corpus cavernosum dose dependently. In the presence of sodium nitroprusside (SNP), DA-8159 significantly sti\mulated the accu\mulation of cGMP when compared to the control level. This indicated that the enhancement of a penile erection by DA-8159 involved the relaxation of the cavernosal smooth \muscle by NO-sti\mulated cGMP accu\mulation. In conclusion, DA-8159 is a selective inhibitor of PDE 5-catalyzed cGMP hydrolysis and the enhancement of a penile erection by DA-8159 is mediated by the relaxation of the cavernosal smooth \muscle by the NO-sti\mulated cGMP accu\mulation.

Molecular and Biochemical Characterization of a Novel Xylanase from Massilia sp. RBM26 Isolated from the Feces of Rhinopithecus bieti

  • Xu, Bo;Dai, Liming;Li, Junjun;Deng, Meng;Miao, Huabiao;Zhou, Junpei;Mu, Yuelin;Wu, Qian;Tang, Xianghua;Yang, Yunjuan;Ding, Junmei;Han, Nanyu;Huang, Zunxi
    • Journal of Microbiology and Biotechnology
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    • v.26 no.1
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    • pp.9-19
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    • 2016
  • Xylanases sourced from different bacteria have significantly different enzymatic properties. Therefore, studying xylanases from different bacteria is important to their applications in different fields. A potential xylanase degradation gene in Massilia was recently discovered through genomic sequencing. However, its xylanase activity remains unexplored. This paper is the first to report a xylanase (XynRBM26) belonging to the glycosyl hydrolase family (GH10) from the genus Massilia. The gene encodes a 383-residue polypeptide (XynRBM26) with the highest identity of 62% with the endoxylanase from uncultured bacterium BLR13. The XynRBM26 expressed in Escherichia coli BL21 is a monomer with a molecular mass of 45.0 kDa. According to enzymatic characteristic analysis, pH 5.5 is the most appropriate for XynRBM26, which could maintain more than 90% activity between pH 5.0 and 8.0. Moreover, XynRBM26 is stable at 37℃ and could maintain at least 96% activity after being placed at 37℃ for 1 h. This paper is the first to report that GH10 xylanase in an animal gastrointestinal tract (GIT) has salt tolerance, which could maintain 86% activity in 5 M NaCl. Under the optimum conditions, Km, Vmax, and kcat of XynRBM26 to beechwood xylan are 9.49 mg/ml, 65.79 μmol/min/mg, and 47.34 /sec, respectively. Considering that XynRBM26 comes from an animal GIT, this xylanase has potential application in feedstuff. Moreover, XynRBM26 is applicable to high-salt food and seafood processing, as well as other high-salt environmental biotechnological fields, because of its high catalytic activity in high-concentration NaCl.

Preparation of minor ginsenosides C-Mc, C-Y, F2, and C-K from American ginseng PPD-ginsenoside using special ginsenosidase type-I from Aspergillus niger g.848

  • Liu, Chun-Ying;Zhou, Rui-Xin;Sun, Chang-Kai;Jin, Ying-Hua;Yu, Hong-Shan;Zhang, Tian-Yang;Xu, Long-Quan;Jin, Feng-Xie
    • Journal of Ginseng Research
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    • v.39 no.3
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    • pp.221-229
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    • 2015
  • Background: Minor ginsenosides, those having low content in ginseng, have higher pharmacological activities. To obtain minor ginsenosides, the biotransformation of American ginseng protopanaxadiol (PPD)-ginsenoside was studied using special ginsenosidase type-I from Aspergillus niger g.848. Methods: DEAE (diethylaminoethyl)-cellulose and polyacrylamide gel electrophoresis were used in enzyme purification, thin-layer chromatography and high performance liquid chromatography (HPLC) were used in enzyme hydrolysis and kinetics; crude enzyme was used in minor ginsenoside preparation from PPD-ginsenoside; the products were separated with silica-gel-column, and recognized by HPLC and NMR (Nuclear Magnetic Resonance). Results: The enzyme molecular weight was 75 kDa; the enzyme firstly hydrolyzed the C-20 position 20-O-${\beta}$-D-Glc of ginsenoside Rb1, then the C-3 position 3-O-${\beta}$-D-Glc with the pathway $Rb1{\rightarrow}Rd{\rightarrow}F2{\rightarrow}C-K$. However, the enzyme firstly hydrolyzed C-3 position 3-O-${\beta}$-D-Glc of ginsenoside Rb2 and Rc, finally hydrolyzed 20-O-L-Ara with the pathway $Rb2{\rightarrow}C-O{\rightarrow}C-Y{\rightarrow}C-K$, and $Rc{\rightarrow}C-Mc1{\rightarrow}C-Mc{\rightarrow}C-K$. According to enzyme kinetics, $K_m$ and $V_{max}$ of Michaelis-Menten equation, the enzyme reaction velocities on ginsenosides were Rb1 > Rb2 > Rc > Rd. However, the pure enzyme yield was only 3.1%, so crude enzyme was used for minor ginsenoside preparation. When the crude enzyme was reacted in 3% American ginseng PPD-ginsenoside (containing Rb1, Rb2, Rc, and Rd) at $45^{\circ}C$ and pH 5.0 for 18 h, the main products were minor ginsenosides C-Mc, C-Y, F2, and C-K; average molar yields were 43.7% for C-Mc from Rc, 42.4% for C-Y from Rb2, and 69.5% for F2 and C-K from Rb1 and Rd. Conclusion: Four monomer minor ginsenosides were successfully produced (at low-cost) from the PPD-ginsenosides using crude enzyme.

Dihydroxy-acid Dehydratase Involved in the Biosynthesis of the Branched-Chain Amino acids, Isoleucine and Valine, from the archaeon Sulfolobus solfataricus

  • Kim, Seong-Hun;Lee, Sun-Bok
    • 한국생물공학회:학술대회논문집
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    • 2005.04a
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    • pp.327-333
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    • 2005
  • Dihydroxy-acid dehydratase (DHAD, 2,3-dihydroxy-acid hydrolyase, EC 4.2.1.9) is one of the key enzymes involved in the biosynthetic pathway of the branched chain amino acid isoleucine and valine. Although the enzyme have been purified and characterized in various mesophiles including bacteria and eukarya, the biochemical properties of DHAD has bee not yet reported from hyperthermophilic archaea. In this study, we cloned, expressed, and purified a DHAD homologue from the thermoacidophilic archaeon Sulfolobus solfataricus P2, which grows optimally at $80\;^{\circ}C$ and pH 3, in E. coli. Characterization of the recombinant S. solfataricus DHAD (rSso_DHAD) revealed that it is the dimeric protein with a subunit molecular weight of 64,000 Da in native structure. rDHAD showed the highest activity toward 2,3-dihydroxyisovaleric acid among 17 aldonic acid substrates Interestingly, this enzyme also displayed 50 % activities toward some pentonic acids and hexonic acids when compared with the activity of this enzyme to the natural substrate. Moreover, rSso_DHAD indicated relatively higher activity toward D-gluconate than any other hexonic acids tested in substrates. $K_m$ and $V_{max}$ values of rSso_DHAD were calculated as $0.54\;{\pm}\;0.04\;mM$ toward 2,3dihydroxyisovalerate and $2.42\;{\pm}\;0.19\;mM$ toward D-gluconate, and as $21.6\;{\pm}\;0.4\;U/mg$ toward 2,3-dihydroxyisovalerate and $13.8\;{\pm}\;0.4\;U/mg$ toward D-gluconate, respectively. In the study for biochemical properties, the enzyme shows maximal activity between $70^{\circ}C$ and $80^{\circ}C$, and the pH range of pH 7.5 to 8.5. The half life time at $80^{\circ}C$ was 30 min. A divalent metal ion, $Mn^{2+}$, was only powerful activators, whereas other metal ions made the enzyme activity reduced. $Hg^{2+}$, organic mercury, and EDTA also strongly inhibited enzyme activities. Particularly, the rSso_DHAD activity was very stable under aerobic condition although the counterparts reported from mesophiles had been deactivated by oxygen.

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Enhanced production of cellulase by a mutant strain of aspergillus phoenicis (Aspergillus phoenicis의 한 돌연변이주에 의한 cellulase의 생성 및 그 특성)

  • 이영록;고상균
    • Korean Journal of Microbiology
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    • v.20 no.3
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    • pp.125-133
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    • 1982
  • Mutational experiments were performed to imporve the cellulase productivity of Aspergillus phoenicis KU175, isolated from the southern part of Korea, as a high cellulase producer. By treatment ultra-violet light nad 4-NQO(4-Nitroquinoline-N-Oxide), mutation waas induced, and treatment ultra-violet light and 4-NQO (4-Nitroquinoline-N-Oxide), mutation was induced, and A.phoenicis KU175-115 was finally selected for its highest avicelase production. Avicelase production of the mutant was increased about 2 times compared with those of the wild strain. However, activities of other hydrolytic enzymes, such as amylase, protease and nuclease, of the mutant strain didn't show a marked difference compared with those of the nuclease, of the mutant strain didn't show a marked difference compared with the wild strain, except slight increase in ribonuclease activity and slight decrease in glucoamylase activity. Avicelases from the mutant strain selected were purified from wheat bran culture by successive salting out, followed by dialysis and column chromatography, and their charcteristics were compared with thosw of the wild strain. Avicelase was separated into three peaks in the mutant strain as well as in the case of wild strain. Avicelase II activity of the mutant strain was prominently higher than that of the wild strain, while avicelase I and III activities of those were equivalent. The optimal pH ranges and stability of avicelase II from the mutant strain were pH4-5 and pH3.5-6.0, respectively, as well as in the case of the wild strain. The optimal temperature and thermal stability of avicelase II from the mutant strain were $40{\sim}50^{\circ}C\;and\;20{\sim}55^{\circ}C$, respectively. These results were same as those of the wild strain. By the using of Eadie-Hofastee plot, $K_m\;and\;V_{max}$ of avicelase II from the mutant and the wild strain were calculated to be 2.29mg/ml and $4.84{\mu}g$ reducing sugar as glucose per min equally, from the line fitted to the data by the least square method. Activity of avicelase II from the mutant strain was slightly activated by $Mg^{++}\;but\;inhibited\;by\;Cu^{++}, \;Mn^{++}\;and\;Zn^{++}$, as well as in the case of the wild strain. Therefore, it was concluded that the mutant didn't induce the formation of another avicelase isozyme, or the changes in the properties of avicelase, but induce the changes in the productively of the same avicelase II by the action of regulatory gane.

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The Promotive Effects of Antioxidative Apigenin on the Bioavailability of Paclitaxel for Oral Delivery in Rats

  • Choi, Sang-Joon;Choi, Jun-Shik
    • Biomolecules & Therapeutics
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    • v.18 no.4
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    • pp.469-476
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    • 2010
  • This study was to investigate the effect of apigenin on the bioavailability of paclitaxel after oral and intravenous administration in rats. The effect of apigenin on P-glycoprotein (P-gp), cytochrome P450 (CYP)3A4 activity was evaluated. The pharmacokinetic parameters of paclitaxel were determined in rats after oral (40 mg/kg) or intravenous (5 mg/kg) administration of paclitaxel with apigenin (0.4, 2 and 8 mg/kg) to rats. Apigenin inhibited CYP3A4 activity with 50% inhibition concentration ($IC_{50}$) of 1.8 ${\mu}M$. In addition, apigenin significantly inhibited P-gp activity. Compared to the control group, apigenin significantly increased the area under the plasma concentration-time curve (AUC, p<0.05 by 2 mg/kg, 59.0% higher; p<0.01 by 8 mg/kg, 87% higher) of oral paclitaxel. Apigenin also significantly (p<0.05 by 2 mg/kg, 37.2% higher; p<0.01 by 8 mg/kg, 59.3% higher) increased the peak plasma concentration ($C_{max}$) of oral paclitaxel. Apigenin significantly increased the terminal half-life ($t_{1/2}$, p<0.05 by 8 mg/kg, 34.5%) of oral paclitaxel. Consequently, the absolute bioavailability (A.B.) of paclitaxel was significantly (p<0.05 by 2 mg/kg, p<0.01 by 8 mg/kg) increased by apigenin compared to that in the control group, and the relative bioavailability (R.B.) of oral paclitaxel was increased by 1.14- to 1.87-fold. The pharmacokinetics of intravenous paclitaxel were not affected by the concurrent use of apigenin in contrast to the oral administration of paclitaxel. Accordingly, the enhanced oral bioavailability by apigenin may be mainly due to increased intestinal absorption caused via P-gp inhibition by apigenin rather than to reduced renal and hepatic elimination of paclitaxel. The increase in the oral bioavailability might be mainly attributed to enhanced absorption in the gastrointestinal tract via the inhibition of P-gp and reduced first-pass metabolism of paclitaxel via the inhibition of the CYP3A subfamily in the small intestine and/or in the liver by apigenin. It appears that the development of oral paclitaxel preparations as a combination therapy is possible, which will be more convenient than the i.v. dosage form.

Investigation on PTCR Characteristics of (1-x)BaTiO3-x(Bi0.5Na0.5)TiO3 (0.01≤x≤0.10) Ceramics by Modified Synthesis Process (수정합성공정에 의한 무연 (1-x)BaTiO3-x(Bi0.5Na0.5)TiO3 (0.01≤x≤0.10) 세라믹의 PTCR 특성 연구)

  • Kim, Kyoung-Bum;Kim, Chang-Il;Jeong, Young-Hun;Lee, Young-Jin;Paik, Jong-Hoo;Lee, Woo-Young;Kim, Dae-Joon
    • Journal of the Korean Institute of Electrical and Electronic Material Engineers
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    • v.23 no.12
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    • pp.929-935
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    • 2010
  • $(1-x)BaTiO_3-x(Bi_{0.5}Na_{0.5})TiO_3$ ($0.01{\leq}x{\leq}0.10$) ceramics were fabricated with muffled sintering by a modified synthesis process. Their positive temperature coefficient of resistivity (PTCR) characteristics were investigated systematically. All specimen showed a perovskite structure with a tetragonal symmetry. Both the lattice parameter of a and c axes were slightly decreased with increasing $(Bi_{0.5}Na_{0.5})TiO_3$ (BNT) content. Grain growth was achieved when the incorporated BNT was increased to 6 mol% and the inhibition of grain growth is considered to be due to the appearance of Ba vacancy ($V^{"}_{Ba}$) in the $(1-x)BaTiO_3-x(Bi_{0.5}Na_{0.5})TiO_3$ ($0.08{\leq}x$). With 4 mol% BNT addition, room temperature resistivity decreased to $48 \Omega{\cdot}cm$ and a resistivity jump ($\rho_{max}/\rho_{min}$) was as high as $1.1{\times}10^4$, respectively. Curie temperature was also increased to $171^{\circ}C$ with increasing BNT content.

High Efficient Inductive Power Supply System Implemented for On Line Electric Vehicles

  • Huh, Jin;Park, Eun-Ha;Jung, Gu-Ho;Rim, Chun-Taek
    • Proceedings of the KIPE Conference
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    • 2009.11a
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    • pp.105-110
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    • 2009
  • The On Line Electric Vehicles(OLEV) that can pick up inductive power from underground coils on driving with high efficiency have been developed this year, and is now proposed in this paper. The IPS(Inductive Power Supply) system consists of power supply inverters, power supply rails, pick up modules, and a regulator. There are 3 generations of IPS have been developed so far, and the $4^{th}$ generation IPS is being developed. The $1^{st}$ generation has been demonstrated this Feb. 27, which is equipped with mechanically auto tracking pick-up module with 1cm air gap, and showed 80% power efficiency. The $2^{nd}$ generation IPS applied to an 120kW (average)/240kW(peak) motor powered electric bus has 17cm air gap with 72% power efficiency. For the $2^{nd}$ generation IPS, the Power supply inverter has 440V, 3phase input and 200A @ 20kHz output. The test power supply rail of 240m long is segmented by 60m each, where newly developed core structure and power cable are constructed under the road covered with asphalt of 5cm thickness. The pick-up modules which consist of core, winding wire, and rectifiers are fixed to the bottom of the bus which can carry more than 40 passengers and can pick up max. 60kW. To remove parasitic component and to transfer maximum power between them resonant circuit topology is applied to the primary and secondary sides. The EMF level is below 62.5mG at 1.75m from the center of the road to meet the regulation. Several effective ways of reducing EMF levels have been developed. In addition, effective ways to solve problems related high frequency power cables buried in ground and it's proof from soil have been studied also. This development shows that the IPS system is capable of supplying enough power to the pick-up of OLEV and can reduce battery size, weight and cost, which means the IPS with OLEV is one of the best candidate for EV.

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Molecular Cloning and Functional Expression of Extracellular Exo-β-(1,3)-Glucanase from Candida fermentati SI (Candida fermentati SI의 exo-β-(1,3)-glucanase유전자의 클로닝 및 그 특성)

  • Lim, Yu-Mi;Kim, Bong-Ki;Kim, Sang-Jun;So, Jai-Hyun;Kim, Won-Chan
    • Microbiology and Biotechnology Letters
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    • v.44 no.3
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    • pp.317-323
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    • 2016
  • An isoflavone glucosidase that catalyzes the hydrolysis of isoflavone glucosides into glucose and corresponding aglycones was purified from Candida fermentati SI. The N-terminal sequence was determined to be GLNCDYCN. We designed degenerate primers on the basis of these amino acid sequences and successfully cloned the full structural gene sequence of the isoflavone glucosidase using inverse PCR. The exo-β-(1,3)-glucanase gene consists of 1227 base-pair nucleotides, encoding a 408-amino-acid sequence that shares 41–96% amino acid homology with other yeast exo-β-(1,3)-glucanases belonging to glycoside hydrolase family 5. The recombinant exo-β-(1,3)-glucanase was expressed in Pichia pastoris X-33, using a pPICZA vector system, and further characterized. The molecular mass of the purified exo-β-(1,3)-glucanase was estimated by SDS-PAGE to be 47 kDa. The optimal pH and temperature were pH 4.5 and 40℃, respectively. The Km values of the purified exo-β-(1,3)-glucanase for daidzin and genistin were 0.12 mM and 0.14 mM, respectively. The Vmax values of the purified isoflavone glucosidase were 945.03 U/mg for daidzin and 835.92 U/mg and for genistin.