• International Journal of Industrial Entomology and Biomaterials
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• v.22 no.2
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• pp.83-93
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• 2011

Biochemical and enzymatic characterization for extracellular protease isolated from Cordyceps militaris cultivated on rice bran medium was investigated. C militaris produced proteolytic enzymes from 10 days after inoculation, maximum enzyme production was found at 25 days. The optimum temperature and pH of proteases production was at $25^{\circ}C$ and pH 7.0, respectively. The protease activity was observed in the four peaks (Pro-I, Pro-II, Pro-III, and Pro-IV) separated through Sephadex G-100 column chromatography. The separated protease was optimally active at $25^{\circ}C$. Optimum pH of the protease was between 7 and 8. Enzyme was also stable over at $30-80^{\circ}C$. The enzyme was highly stable in a pH range of 4-9. Protease activity was found to be slightly decreased by the addition of $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Fe^{2+}$ and $Cu^{2+}$, whereas inhibited by the addition of $Ca^{2+}$ and $Co^{2+}$ Protease activity was inhibited by protease inhibitor PMSF. On the other hand, the partially purified protease was investigated on proteolytic protease activity by zymogram gel electrophoresis using three substances (casein, gelatin and fibrin). Four active bands (F-I, FII, F-III, and F-IV) of fibrin degradation were revealed on fibrin zymogram gels. Both of F-II and FIII showed caseinolytic, fibrinolytic and gelatinolytic activities in three gels. Thermostability, pH stability, and pH-thermostability of the enzyme determined the residual fibrinolytic activity also displayed on fibrin zymogram gel. The only one enzyme (F-II) displayed over a broad range of temperature at $30-90^{\circ}C$. The FII displayed fibrinolytic activity in the pH range 3-5, but was inactivated in the range of pH 6-11. The F-I and F-III showed enzyme activity in the pH range of 6-11. In the pH-thermostability, the F-II only kept fibrinolytic activity after heating at $100^{\circ}C$ for 10, 20 and 30 min at pH 3 and pH 7, respectively. On the other hand, the F-II was retained activity until heating for 10 min under pH 11 condition. By using fibrin zymogram gel electrophoresis, extracellular fibrinolytic enzyme F-II from C. militaris showed unusual thermostable under acid and neutral conditions.

• Journal of Animal Science and Technology
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• v.46 no.2
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• pp.251-260
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• 2004

The feasibility and stability of ORP, pH(mV) and DO as a real-time control parameter for SBR process were evaluated in this study. During operation, NBP(nitrogen break point) and NKP(nitrate knee point), which reveal the biological and chemical changes of pollutants, were clearly observed on ORP and pH(mV)-time profiles, and those control points were easily detected by tracking the moving slope changes(MSC). However, when balance of aeration rate to loading rate, or to OUR(oxygen uptake rate), was not optimally maintained, either false NBP was occurred on ORP and DO curves before the appearance of real NBP or specific NBP feature was disappeared on ORP curve. Under that condition, however, very distinct NBP was found on pH(mV)-time profile, and stable detection of that point was feasible by tracking MSC. These results might mean that pH(mV) is superior real-time control parameter for aerobic process than ORP and DO. Meanwhile, as a real-time control parameter for anoxic process, ORP was very stable and more useful parameter than others. Based on these results, a stable real-time control of process can be achieved by using the ORP and pH(mv) parameters in combination rather than using separately. A complete removal of pollutants could be always ensured with this real-time control technology, despite the variations of wastewater and operation condition, as well as an optimization of treatment time and capacity could be feasible.

• Journal of the Korean Applied Science and Technology
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• v.33 no.3
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• pp.599-605
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• 2016

Serratia marcescens, a Gram-negative bacterium characterized by production of a nondiffusible red pigment. Serratia marcescens 2354 (ATCC 25419) was production and purification a high concentration of red pigments when growing on Cang's soytone (CS) culture broth with soytone and ethanol. The optimal temperature and intial pH range for the production of the red pigments were $28^{\circ}C$ and pH 7.5, respectively. The red pigments was separated and purified through organic solvents extraction. Characterization of the red pigments is studied by UV-spectrophotometer at ${\lambda}_{max}$ 537 nm. The HPLC-Mass analysis of the partially purified compounds showed two major peaks with the molecular masses of 537 and 565 g. The red pigments were stable at room temperature under the acidic pH (up to pH 6) but were unstable at the strong alkaline condition. And red pigments were stable at sun light.

• Journal of Microbiology and Biotechnology
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• v.19 no.10
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• pp.1077-1084
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• 2009

A genomic library was constructed to clone a xylanase gene (Mxyn10) from Demequina sp. JK4 isolated from a deep sea. Mxyn10 encoded a 471 residue protein with a calculated molecular mass of 49 kDa. This protein showed the highest sequence identity (70%) with the xylanase from Streptomyces lividans. Mxyn10 contains a catalytic domain that belongs to the glycoside hydrolase family 10 (GH10) and a carbohydrate-binding module (CBM) belonging to family 2. The optimum pH and temperature for enzymatic activity were pH 5.5 and $55^{\circ}C$, respectively. Mxyn10 exhibited good pH stability, remaining stable after treatment with buffers ranging from pH 3.5 to 10.0. The protein was not significantly affected by a variety of chemical reagents, including some compounds that usually inhibit the activity of other related enzymes. In addition, Mxyn10 showed activity on cellulose. These properties mark Mxyn10 as a potential enzyme for industrial application and saccharification processes essential for bioethanol production.

• Microbiology and Biotechnology Letters
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• v.21 no.5
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• pp.440-445
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• 1993

The fungi SFN 416 strain which produced a stable beta-glucosidase was isolated from nature and identified to Aspergillus niger. Optimal conditions of enzyme reaction were temperature 36C, pH-5.0, reaction time-40 minutes. The enzyme was stable below 60C and in the range of pH 4.5-6.5. The enzyme was greatly inhibitied by Ag+ and slightly activated by Ca2+ (0.5mM) and Cu2+ (5 mM).

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.243-249
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• 1975

This experiment were carried out to investigate the conditions of amylase produced by Candida muscorum in wheat bran cultures and the properties of its amylase (crude enzyme). The results obtained were as follows. 1. The optimum conditions for amylase production in wheat bran cultures were; water content 75 percent, temperature $25^{\circ}C$ and incubation time 4-7 days. 2. The production of amylase was increased about 20 percent in the medium added 0.5 percent of ammonium sulfate or ammonium chloride to wheat bran, but the production of those was decreased in the case of addition of nitrates. 3. No significant effect was found in the case of the addition of carbon source on the production of amylase. 4. The properties of liquefying amylase of the selected strain were; the optimum pH 4.2, the optimum temperature $60-65^{\circ}C$, the stable pH 3.2-6.8 and the stable heating (for 15 minutes heating) below $65^{\circ}C$. 5. The properties of saccharifying amylase of the selected strain were; the optimum pH 4.5, the optimum temperature $55^{\circ}C$, the stable pH 3.8-6.2 and the stable heating (for 15 minutes heating) below $45^{\circ}C$.

• Bulletin of the Korean Mathematical Society
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• v.34 no.1
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• pp.1-8
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• 1997

Let G be a finiteg oroup. We denote BG a classifying space of G, which a contractible universal principal G bundle EG. The stable type of BG does not determine G up to isomorphism. A simple example [due to N. Minami]is given by $Q_{4p} \times Z/2$ and $D_{2p} \times Z/4$ where ps is an odd prime, $Q_{4p} is the generalized quarternion group of order 4p and $D_{2p}$ is the dihedral group of order 2p. However the paper [6] gives us a necessary and sufficient condition for $BG_1$ and $BG_2$ to be stably equivalent localized et pp. The local stable type of BG depends on the conjegacy classes of homomorphisms from the p-groups Q into G. This classification theorem simplifies if G has a normal sylow p-subgroup. Then the stable homotopy type depends on the Weyl group of the sylow p-subgroup.

• Journal of Microbiology and Biotechnology
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• v.11 no.4
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• pp.558-563
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• 2001

A new alkalophilic strain of Bacillus pumilus JB¬05 producing bleach-stable and halo-tolerant alkaline protease was isolated from cement industry effluents in Karnataka, India. The effects of carbon and nitrogen sources on protease production by this alkalophilic strain were observed after a 30-h incubation. A high level of alkaline protease activity was obtained in the presence of starch as the carbon and peptone as the nitrogen sources. The partially purified enzyme showed an optimum temperature and pH activity at $58^{\circ}C$ and 10.5, respectively. The enzyme was completely inhibited by PMSF (95.0%) indicating it as a serine protease. It is bleach-stable as it retained 35% original activity in the presence of 10% (v/v) hydrogen peroxide at $30^{\circ}$C after 2 h and is halo-tolerant as it retained 70% original activity in the presence of 2.5 M sodium chloride at $30^{\circ}C$ after 2 h incubation.

• Bulletin of the Korean Chemical Society
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• v.5 no.4
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• pp.149-153
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• 1984

Reactions of $MoOCl_5^{2-}$ with ${\alpha}_2-[P_2W_{17}O_{61}]^{10-}$ have been studied spectrophotometrically and several complexes have been identified. The transient species initially formed is probably $[Mo_2O_4(P_2W_{17}O_{6l})_2]^{18-}$. At $pH {\le} 3$the visible spectrum changes gradually, indicating formation of a transient isomer of $[P-2Mo^VW_{17}O_{62}]^{7-}$, which again transforms into the stable isomer. The transient isomer absorbs light much more strongly than the stable isomer in the visible range. At $pH > 3 [P_2W^VW_{16}O_{61}]^{11-}$ is formed probably via the transient isomer of $[P_2Mo^VW_{17}O_{61}]^{7-}$.

• Journal of Life Science
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• v.25 no.5
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• pp.496-506
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• 2015

This study explored adequate water temperature ranges for maintaining stable water quality in a biofloc- based zero-water exchange culture system. Five experimental tanks with the following temperatures were set up: 10℃, 15℃, 20℃, 25℃, and 30℃. First, a biofloc-based culture system was developed in the experimental tanks; then, the tanks were stocked with goldfish and went without a water exchange for 60 days. Conditions for developing a biofloc-based culture system and stable water quality in low concentrations of inorganic nitrogen compounds at 10℃, 15℃, 20℃, 25℃, and 30℃ were maintained after 17, 26, 43, 68, and 78 days, respectively. Beginning from when the goldfish were stocked in the biofloc-based culture tanks, concentrations of $NH_4{^+}-N$ remained constant and at low levels at 10℃ and 15℃, but they showed a gradual increase at 20℃, 25℃, and 30℃. Concentrations of $NO_2{^-}-N$ and $NO_3{^-}-N$ at 10℃ and 15℃ did not remain at low levels and immediately increased. While $NO_2{^-}-N$ concentrations at above 20℃ remained constant and stable at relatively low levels, $NO_3{^-}-N$ concentrations showed a gradual increase. Conditions of 15℃ and below could not maintain low and stable concentrations of $NO_2{^-}-N$. In the pH range of 4.0 to 6.0, $NH_4{^+}-N$ concentration decreased as the pH rose. However, there was no correlation between pH and $NH_4{^+}-N$ concentration in the pH range of 6.0 to 8.0. These results indicate that pH levels should be kept at pH 6.0 and above to maintain a low and stable concentration of $NH_4{^+}-N$ at above 20℃.