• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.258-263
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• 1998

${\beta}$-Xylosidase was purified from the recombinant Escherichia coli carrying the Bacillus sp. KK-1 ${\beta}$-xylosidase gene (xylB). The molecular mass of the purified enzyme was estimated to be 62 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, the apparent molecular mass of the ${\beta}$-xylosidase was 140 kDa, indicating that the native ${\beta}$-xylosidase has an oligomeric structure composed of two identical subunits. The isoelectric point was determined to be pH 5.5. The enzyme was highly active on p-nitrophenyl-$\beta$-D-xylopyranoside but it barely hydrolyzed xylan substrates, and did not exhibit activity towards carboxymethylcellulose and p-nitrophenyl-${\beta}$-D- glucopyranoside. The enzyme had a pH optimum for its activity at pH 6.5 and a temperature optimum at $40^{\circ}C$. The enzyme activity was completely inhibited by the presence of $Hg^{++}$, and also markedly inhibited by D-xylose and D-glucose.

• Food Science and Biotechnology
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• v.18 no.6
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• pp.1342-1350
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• 2009

This paper investigates the production and optimization of $\beta$-galactosidase enzyme using synthetic medium by Kluyveromyces lactis NRRL Y-8279 in stirred tank bioreactor. Response surface methodology was used to investigate the effects of fermentation parameters on $\beta$-galactosidase enzyme production. Maximum specific enzyme activity of 4,622.7 U/g was obtained at the optimum levels of process variables (aeration rate 2.21 vvm, agitation speed 173.4 rpm, initial sugar concentration 33.8 g/L, incubation time 24.0 hr). The optimum temperature and pH of the $\beta$-galactosidase enzyme produced under optimized conditions were $37^{\circ}C$ and pH 7.0, respectively. The enzyme was stable over a pH range of 6.0-7.5 and a temperature range of $25-37^{\circ}C$. The $K_m$ and $V_{max}$ values for O-nitrophenol-$\beta$-D-galactopyranoside (ONPG) were 1.20 mM and $1,000\;{\mu}mol/min{\cdot}mg$ protein, respectively. The response surface methodology was found to be useful in optimizing and determining the interactions among process variables in $\beta$-galactosidase enzyme production. Hence, this study fulfills the lack of using mathematical and statistical techniques in optimizing the $\beta$-galactosidase enzyme production in stirred tank bioreactor.

• Journal of Pharmaceutical Investigation
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• v.27 no.3
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• pp.219-223
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• 1997

Terfenadine, antihistaminic drug, is poorly soluble in water. The purpose of this study is to investigate the possibility of using $terfenadine-{\beta}-cyclodextrin$ inclusion compound, instead of terfenadine, as the active substance of solid dosage form by improving the solubility, dissolution and anti-histaminic activity of terfenadine. The solubility and binding characteristics of $terfenadine-{\beta}-cyclodextrin$ complex in pH $1.2{\sim}6.8$ were investigated. Furthermore, the preparing method of $terfenadine-{\beta}-\;cyclodextrin$ inclusion compound was setting up and its physico-chemical characteristics such as DSC curve, solubility, dissolution and anti-histaminic activity were investigated. In conclusion, the solubility of terfenadine was increasing ${\beta}-cyclodextrin$ and with the decreasing pH. $Terfenadine-{\beta}-cyclodextrin$ inclusion compound, whose yield is almost 100%, was prepared by neutralization method. This inclusion compound was 200-times as soluble as terfenadine in pH 1.2-6.8. In addition, it had the faster dissolution and anti-histaminic activity than terfenadine. Therefore, it is used to the active substance of solid dosage form such as tablet and capsule in stead of terfenadine.

• Korean Journal of Microbiology
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• v.22 no.2
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• pp.77-84
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• 1984

This examined some conditions for the induction of ${\beta}$-D-galactosidase synthesis in Candida kefyr CBS 834. The optimal pH, temperature, and inoculum size either for growth or${\beta}$-D-galactosidase synthesis were 5.5, $30^{\circ}C$ and above 0.2 at A610nm, respectively. Enzyme activity began to increase at 2h after the addition of inducer, and continued to increase linearly up to $2{\sim}3h$ before reaching stationary phase, and thereafter its activity was decreased. ${\beta}$-D-galactosidase was induced either by lactose or galactose but not either by glucose or ethanol. The greater activity of ${\beta}$-D-galactosidase on galactose than on lactose indicated that the former might be natural inducer for ${\beta}$-D-galactosidase synthesis. The rate of its induction as a function of lactose concentration showed that enzyme activity increased linearly above 4mM, while it was very low below that. Glucose represed the induction of ${\beta}$-D-galactosidase, and the period of adaptation to inducer from other carbon sources was relatively short.

• Archives of Pharmacal Research
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• v.12 no.1
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• pp.42-47
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• 1989

From the roots of Puisatiila koreana, three monodesmosides(pulsatilla saponins A, B and D) and two bisdesmosides(pulsatilla saponins F and H) were isolated. The structure of these saponins have been determined as hederagenin 3-O-${\beta}$-L-rhamnopyranosyl($1{\to}2$)- ${\alpha}$-L-arabinopyranoside(A), hederagenin 3-O-${\beta}$-D-glucopyrano syl($1{\to}4$) - ${\alpha}$-L-arabinopyranoside(B), hederagenin 3-O- ${\alpha}$-L-rhamnopyranosyl ($1{\to}2$)-[${\beta}$-D-glucopyranosyl($1{\to}4$]-${\alpha}$-L-arabinopyranoside(D), 3-O-${\alpha}$-L-rhamnopyranosyl($1{\to}2$)-{${\alpha}$-L-arabinopyranosyl hederagenin 28-O-${\alpha}$-L-rhamnopyrano syl($1{\to}4$)-${\beta}$-D-glucopyrano syl($1{\to}6$)-${\beta}$-D-glucopyranosyI ester (F) and 3-O-${\alpha}$-L-rhamnopyranosyl($1{\to}2$)-[${\beta}$-D-glucopyranosyl($1{\to}4$)]- ${\alpha}$-L-arabinopyranosyl hederagenin 28-O-${\alpha}$-L-lharnnopyranosyl($1{\to}4$)-${\beta}$-D-glucopyranosyl($1{\to}6$)-${\beta}$-D-glucop yranosyl ester(H) on the basis of chemical and spectral studies. Pulsatilla saponin B is the first report of its presence in plants but saponins A, D, F, and H have recently been isolated from the same genus p. cernua.

• The Korean Journal of Food And Nutrition
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• v.13 no.4
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• pp.342-347
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• 2000

The stabilization of barley $\beta$-amylase(Biozyme ML, Amano) was attained by modification with periodate-oxidized soluble starch. The specific activities of modified enzyme at pH 9.7 and pH 8.0 were 42% and 92%, respectively, compared with that of native enzyme. The pH stability of modified enzyme was increased at pH 2~5 and 7~12 in the presence of $\alpha$-cyclodextrin( $\alpha$ -CD) compared wish that of native enzyme. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 10min. the activity remained 8% for the enzyme modified at pH 8.0 in the presence of $\alpha$-CD, 4.5% for the native enzyme. The native enzyme and modified enzyme showed two peak in HPLC. The molecular weight of the modified enzyme was slightly increased in HPLC analysis.

• Journal of the Korean Society of Clothing and Textiles
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• v.23 no.3
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• pp.353-360
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• 1999

An investigation made of the variations of angle of bias on the top of the sleeve cap curve line and calculated easing contraction ratio by capheights(A ; a,h$\times$5,/6) B: A, H/4 +4cm C:A.H/3 D: A.H/ 4+3cm E:AH/4+2cm, F: A,H/4+1cm, G: A,H/4, H:A,H/6, I:A,H/8) and the efects of easing contraction on the cap curve lines of sleeve A, D, G by easing stitch density with the gathering foot: sewing condition-lockstitch industrial machine stitch density(N1.0 ; 38stitches/3cm N1.5: 26stitches/3cm, N2.0 ; 19stitches/3cm, N2.5 ; 14stitches/ 3cm) The results obtained were as follows; 1) The variations of the angle of bias on the top of the sleeve cap curve line by cap heights can be done according to the angle balance (front; $\alpha$-$\beta$ back ; $\alpha$'- $\beta$') between the angle (front ;$\alpha$, $\beta$, back ; $\alpha$'- $\beta$') of bias of the two base-lines. 2) The higher cap height the more higher the calculated easing contraction ratio. 3) The lower the stitch density the higher easing contraction ratio. 4) The effects of easing contraction was that sleeve G was more than sleeve A, D.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.1
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• pp.50-56
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• 2002

The $\beta$-galactosidase was purified from the internal organs of edible snail by fractionation with ammonium sulfate, ion exchange chromatography on DEAE-Sephadex, Mono Q HR 5/5 and gel filtration on Sephacryl S-200. Superose 12 HR 10/30 chromatography. The specific activity of the purified $\beta$-galactosidase was 18.8 units/mg protein with 31.3 purification fold from crude extract. The $\beta$-galactosidase had native molecular weight of 144,000 dalton and was composed of two subunits of 72,000 dalton. The isoelectric point of the enzyme was determined 4.1. This enzyme was the most active at pH 3.0 and 6$0^{\circ}C$, and was stable in the pH range 2.0~8.0 and below 5$0^{\circ}C$. The enzyme was inhibited by metal ions and sugars such as fructose, glucose, galactose, maltose and xylose.

• Korean Journal of Food Science and Technology
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• v.17 no.4
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• pp.240-244
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• 1985

Curde $\beta$-amylase was prepared by frationation of the water extracts from Korean ginseng, Panax Ginseng C.A. Meyer, with 0.2-0.6 saturation of ammonium sulfate. The enzyme showed the typical properties of $\beta$-amylase, producing only maltase from starch. The enzyme preparation also showed no maltase activity. The enzyme was stable at the pH 5-9 and at the temperature below $40^{\circ}C$. The enzyme showed the optimum pH at 5.0 and the optimum temperature at $35^{\circ}C$. Its activities had proportional relations with substrate concentration below 12 mg%, showing Km V slues of 4.76 mg%. The enzyme was inhibited by $Ag^{+}$, $Hg^{++}$, $Cd^{++}$, $Cu^{++}$,$ Al^{3+}$, and $Fe^{3+}$.

• Journal of Embryo Transfer
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• v.21 no.3
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• pp.247-253
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• 2006

본 연구는 안정된 돼지 체외 성숙 난자를 얻을 목적으로 배양액의 종류 및 배양액에 EGF, ${\beta}-ME$, 호르몬 첨가가 돼지 난포란의 체외 성숙에 미치는 영향을 조사하였다. 난포란을 TCM-199, NCSU-23 및 PZM-3으로 48시간 배양했을 때 체외 성숙율은 각각 $22.1{\pm}0.70%,\;30.6{\pm}0.70%$ 및 $30.4{\pm}2.82%$였다. TCM-199로 48시간 배양했을 때 체외 성숙율은 NCSU-23 및 PZM-3 보다 약간 낮은 체외 발생율을 나타냈다. 난포란을 25 ng/ml의 EGF를 첨가한 TCM-199, NCSU-23 및 PZM-3로 48시간 배양했을 때 체외 성숙율은 각각 $46.3{\pm}2.8%,\;76.6{\pm}3.1%$ 및 $72.2{\pm}2.6%$로 나타났다. 난포란의 배양 시 배양액에 25 및 50 ng/ml의 EGF를 첨가 후 48시간 배양했을 때 첨가하지 않은 군에 비해 높은 체외 성숙율을 나타냈다(p<0.05). 난포란을 NCSU-23 및 PZM-3 배양액에 $25{\mu}M/ml$의 ${\beta}-ME$를 첨가한 후 48시간 배양했을 때 체외성숙율은 각각 $43.9{\pm}1.41%,\;41.7{\pm}l.41%,\;44.4{\pm}0.70%,\;40.6{\pm}0.70%$로 나타났다. 난포란을 $25{\mu}M/ml$의 ${\beta}-ME$를 첨가한 NCSU-23로 48시간 배양했을 때 첨가하지 않은 군에 비해 높은 체외 성숙율을 나타냈다(p<0.05). 난포란의 배양 시 NCSU-23에 PMSG, hCG, PMSG+hCG, hCG+${\beta}$-estradiol, PMSG+${\beta}$-estradiol을 첨가 후 배양하였을 때 체외 성숙율은 각각 75.6%, 77.8%, 80.0%, 86.4% 및 84.8%로서 무첨가 군(64.4%)에 비해 높게 나타났다(p<0.05).