• Journal of Microbiology and Biotechnology
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• v.33 no.4
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• pp.533-542
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• 2023

Exo-polygalacturonase (exo-PG) hydrolyzes pectin acids and liberates mono-galacturonate, which plays an important role in juice extraction, and has rarely been reported. Exo-PG (AfumExoPG28A) from Aspergillus fumigatus belongs to the glycoside hydrolase 28 family. In this study, its gene was cloned and the protein was expressed and secreted in Pichia pastoris with a maximal activity of 4.44 U/ml. The optimal temperature and pH of AfumExoPG28A were 55℃ and 4.0, respectively. The enzyme exhibited activity over almost the entire acidic pH range (>20.0% activity at pH 2.5-6.5) and remained stable at pH 2.5-10.0 for 24 h. The K_m and V_max values of AfumExoPG28A were calculated by the substrate of polygalacturonic acid as 25.4 mg/ml and 23.6 U/mg, respectively. Addition of AfumExoPG28A (0.8 U/mg) increased the light transmittance and juice yield of plantain pulp by 11.7% and 9%, respectively. Combining AfumExoPG28A (0.8 U/mg) with an endo-PG (0.8 U/mg) from our laboratory, the enzymes increased the light transmittance and juice yield of plantain pulp by 45.7% and 10%, respectively. Thus, the enzyme's potential value in juice production was revealed by the remarkable acidic properties and catalytic activity in fruit pulp.

• Journal of Plant Biology
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• v.29 no.1
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• pp.53-65
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• 1986

The montane forests of Ulreung Island, Korea, were investigated by the ZM school method. By comparing the montane forests of this island with those of Korean Peninsula and of Japan, a new order, F a g e t a l i a m u l t i n e r v i s, a new alliance, F a l g i o n m u l t i n e r v i s, a new association, H e p a t i c o-F a g e t u m m u l t i n e r v i s and Rhododendron brachycarpum-Pinus parviflora community were recognized. The H e p a t i c o - F a g e t u m m u l t i n e r v i s was further subdivided into four subassociations; Subass. of Sasa kurilensis, Subass. of Rumohra standishii, Subass. of Rhododendron brachycarpum and Subass. of typicum. Each community was described in terms of floristic, structural and environmental features.

• Bulletin of the Korean Mathematical Society
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• v.26 no.1
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• pp.1-9
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• 1989

In 1980 and 1983, it was proved that P $D^{2}$-groups are surface groups ([2], [3]). Since then, topologists have been positively studying about P $D^{n}$ -groups (or $D^{n}$ -groups). For example, let a topological space X have a right .pi.-action, where .pi. is a multiplicative group. If each x.memX has an open neighborhood U such that for each u.mem..pi., u.neq.1, U.cap. $U_{u}$ =.phi., this right .pi.-action is said to be proper. In this case, if X/.pi. is compact then (1) .pi.$_{1}$(X/.pi).iden..pi.(X:connected, .pi.$_{1}$: fundamental group) ([4]), (2) if X is a differentiable orientable manifold with demension n and .rho.X (the boundary of X)=.phi. then $H^{k}$ (X;Z).iden. $H_{n-k}$(X;Z), ([6]), where Z is the set of all integers.s.

• KSBB Journal
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• v.17 no.4
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• pp.381-387
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• 2002

A filamentous fungus, strain FB01 showing high $\beta$-glucosidase activity was isolated from a compost. This fungus was cocultured with Trichoderma viride to enhance the productivity of $\beta$-glucosidase by changing inoculation time of the fungus. The microbial consortium showed higher cellulolytic enzyme production than T. viride alone. The maximal enzyme production was obtained when the microbial consortium was cultured at 30$\^{C}$ and pH 6.0 for 10 days with the activities of CMCase, $\beta$-glucosidase, and avicelase of 2.0, 0.8, and 0.2 U/mL, respectively. These enzyme activities were 2, 4, and 2 times as high as those of CMCase, p-glucosidase, avicelase from T. viride, respectively, indicating that a synergistic interaction appeared between T. viride and strain FBOI . The serial subcultures with pH control increased $\beta$-glucosidase production about 3.2 times. Enzyme production using ricestraw as a carbon source showed that the activities of CMCase, $\beta$-glucosidase, and avicelase were 3.69, 0.76, 0.17 U/mL, respectively, and $\beta$-glucosidase activity was 1.5 times higher than that of T viride.

• Microbiology and Biotechnology Letters
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• v.32 no.4
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• pp.307-311
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• 2004

Hot water soluble extract from sporophyll of Undaria pinnatifida was examined for antioxidant activity using l,l-diphenyl-picrylhydrazyl (DPPH) and lipid peroxidation assay. The $IC_{50}$ value (7.6 mg/ml) of hot water extract from sporophyll of U. pinnatifida was more higher than ascorbic acid (0.025 mg/ml) and BHT (0.25 mg/ml). The hot water extract from sporoof U. pinnatifida was stable from pH 2 to pH 7 but decreased at alkali pH. The heat stability of hot water extract from sporophyll of U. pinnatifida was stable from $0^{\circ}C$ to $120^{\circ}C$. An effect on an antioxidant activity of hot water extract from sporophyll of U. pinnatifida was studied with various metal ions and EDTA. Antioxiactvity of hot water extract from sporophyll of U. pinnatifida was inhibited by EDTA but increased by adding $Cu^{2+}$, $Co^{2+}$ and $Mn^{2+}$, respectively.

• Proceedings of the Korean Institute of Surface Engineering Conference
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• 2009.05a
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• pp.141-141
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• 2009

흑색 3가크롬용액을 최적의 전착조건을 찾기 위해서 pH와 온도의 변화에 따란 Hull-cell test, 두께측정, 분극실험을 실시하였다. 온도가 올라갈수록, pH가 낮을수록 도금층의 두께가 두꺼워졌으나, 온도 $40^{\circ}C$, pH 3.4-3.8일때 균일한 도금층을 얻을 수 있었다.

• Korean Journal of Crystallography
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• v.9 no.2
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• pp.149-152
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• 1998

The accurate expression of the anisotropic thermal parameters is either exp (-2$π^{2}$ < $h^{2}$ $\frac{$u_x^2$}{$a^{2}$}$ + $k^{2}$ $\frac{$u_y^2$}{$b^{2}$}$ + $l^{2}$ $\frac{$u_z^2$}{$c^{2}$}$ + 2hk $\frac{$u_{x}}{a}$ $\frac{$u_{y}}{b}$ 2hl $\frac{$u_{x}}{a}$ $\frac{$u_{z}}{c}$ 2kl $\frac{$u_{y}}{b}$ $\frac{$u_{z}}{c}$ > ) with the small displacements Ux, Uy, uz, in absolute measure or exp (-2$π^{2}$ < $h^{2}$ $u_x^2$ + $k^{2}$ $u_y^{2}$ + $l^{2}$ $u_z^{2}$ + 2hk$u_{x}$ $u_{y}$ + 2hl$u_{x}$$u_{z}$ + 2kl$u_{y}$ $u_{z}$ > ) with the small displacements Ux, Uy, Uz in fractional measure.

• Analytical Science and Technology
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• v.10 no.4
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• pp.282-290
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• 1997

The sorption and desorption properties of U(VI), Th(IV), Zr(IV), Cu(II), Pb(II), Ni(II), Zn(II), Cd(II) and Mn(II) ions on XAD-16-[4-(2-thiazolylazo)orcinol] (TAO) chelating resin were studied by elution method. The effect was examined with respect to overall capacity of each metal ion, separation of mixed metal ions, flow rate and concentration of buffer solution for optimum condition of sorption. The overall capacities of some metal ions on this chelating resin were 0.35nmol U(VI)/g resin, 0.49nmol Th(IV)/g resin, 0.41nmol Cu(II)/g resin, and 0.31nmol Zr(IV)/g resin, respectively. The elution order of metal ions obtained from breakthrough capacity and overall capacity at pH 5.0 was Th(IV)>Cu(II)>U(VI)>Zr(IV)>Pb(II)>Ni(II)>Zn(II)>Mn(II)>Cd(II). The group separation of mixed metal ions was possible by increasing pH in pH range 2~5 at a flow rate of 0.28mL/min. Characteristics of desorption were investigated with desorption agents such as $HNO_3$, HCl, $HClO_4$, $H_2SO_4$, and $Na_2CO_3$. It was found that 2M $HNO_3$ showed high desorption efficiency to most of metal ions except Zr(IV) ion. Also, desorption and recovery of Zr(IV) ion were successfully performed with 1M $H_2SO_4$. Recovery of trace amount of U(VI) ion from artificial sea water was over 94%. The chelating resin, XAD-16-TAO was successfully applied to group separation of rare earth metal ions from U(VI) by using 2M $HNO_3$ as an eluent.

• Korean Journal of Microbiology
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• v.19 no.1
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• pp.31-37
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• 1981

Avicelase, CMCase and salicinase of A.phoenicis K.U. 175 were purified from wheat bran culture by salting out with ammonium sulfate, dialysis and successive column chromatography Sephadex G-100. Optimum pH and temperature of avicelase were pH 3.8-4.8, $35-55^{\circ}C$ and that of CMCase, salicinase were pH4.5-5.5, $45-60^{\circ}C$ and pH 4.5-6.0, $45-60^{\circ}C$ respectively. These enzymes were relatively thermostable, alkali unstable and inhibited by $Ca^{++},\;Mn^{++},\;Cu^{++},\;and\;Hg^{++}$. Km values of avicelase, CMCase and salicinase were calculated to be $1.5{\times}10^{-4}M,\;5.5{\times}10^{-4}M\;and\;2.75{\times}10^{-5}M$ and Vmax values $1.66{\times}10^{-4}mM/min,\;3.33{\times}10^{-4}mM/min\;and\;1.14{\times}10^{-4}mM/min$, respectively.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.585-590
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• 1990

The cyclodextrin glucanotransferase (CGTase) was purified from the culture broth of Bacillus stearothermophilus by ammonium sulfate precipitation and affinity chromatography. The specific activity of the CGTase increased by about 31-fold from 111.5 U/mg protein to 3445.0 Ulmg protein. The SDSPAGE indicated that the purified CGTase was homogeneous and the molecular weight of the purified CGTase was about 78,000. The optimum pH and temperature was 6.0 and $60^{\circ}C$, respectively. This enzyme was stable from pH 5.5-10.0. The enzyme retained its full activity at the incubation temperature up to $60^{\circ}C$ and calcium ion increased the thermal stability. The isoelectric point was about 4.8.