• Archives of Pharmacal Research
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• v.2 no.2
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• pp.79-83
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• 1979

Using cephalosporium acremonium ATCC 14553, we studied on the important factors in fermentation. Those factors were :carbon and nitrogen sources, methionine effect, absorbent effect, fermentation variables in a batch fermentation variables in a batch fermentation, effect of reuse of its cellular biomass as a reusable nutrient, and 2, 4-dinitrophenol effect on cephalosprin C production.

• Bulletin of the Korean Chemical Society
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• v.29 no.6
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• pp.1157-1161
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• 2008

2,6-Dinitrophenol (2,6-DNP) complexes with lanthanide series including yttrium (except Pm, Tm, and Lu) have been synthesized and their crystal structures have been analyzed by X-ray diffraction methods. Singlecrystal X-ray structure determinations have been performed at 296 K on the Ce$\rightarrow$Yb species and shown them to be isomorphous, triclinic, P1, a = 8.6558(2)$\rightarrow$8.5605(3) $\AA$, b = 11.8813(3)$\rightarrow$11.6611(4) $\AA$, c = 13.9650(3) $\rightarrow$13.8341(5) $\AA$, $\alpha$ = 73.785(1)$\rightarrow$73.531(2)o, $\beta$ = 74.730(1)→74.903(2)${^{\circ}}$, $\gamma$ = 69.124(1)→ 69.670 $(2){^{\circ}}$, V = 1266.86(5)→1221.53(7) $$\AA^{3}$$, Z = 2. In Ln(III) complexes, three 2,6-DNP ligands coordinate directly to the metal ion in the bidentate fashion. The nine coordinated Ln(III) ion forms slightly distorted tri-capped trigonal prism. There are no water molecules in the crystal lattice. The dependences of metal to ligand bond lengths are discussed on the atomic number of lanthanide elements. The thermal properties of lanthanide complexes of 2,6- DNP have also studied by TG-DTG and DSC thermal analysis methods.

• Microbiology and Biotechnology Letters
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• v.2 no.1
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• pp.13-17
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• 1974

A strain of Streptomyces sp. which producing a metal containing proteolytic enzyme was isolated from soil and some properties of this enzyme were investigated. The following results were obtained. 1. Optimal pH and temperature of this enzyme were pH7.0 and 37$^{\circ}C$ 2. This enzyme was easily inactivated with heat treatment: for example, by the treatmentat 37$^{\circ}C$ for 100 minutes the activity of the enzyme was decreased to about 50 per cent of intial actively but this enzyme was stable at neutral pH. 3. The activity of this enzyme was not inhibited by $Mg^{＋＋}$, $_Mn^{＋＋}$, $Ca^{＋＋}$, Pb$^{＋＋}$, or $Ba^{＋＋}$ ect. but strongly inhibited by Hg$^{＋＋}$, Co$^{＋＋}$, Ag$^{＋}$, Cu$^{＋＋}$, or Cd$^{＋＋}$. 4. This enzyme was strongly inhibited by EDTA but was not inhibited by oxalic acid, citric acid, 2, 4-dinitrophenol, $\varepsilon$-aminocaproic acid, cysteine, or thiourea.

• Applied Biological Chemistry
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• v.37 no.5
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• pp.356-360
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• 1994

The optimum pH and temperature for endo-polygalacturonase activity from Jujube were 5.0 and $50^{\circ}C$. The range of its stability to pH was 4.0 to 5.0. The enzyme was inactivated about 35% by treatment at $70^{\circ}C$ for 1 hr. It was found that $Ag^+$, $Zn^{++}$ and $Mg^{++}$ increased the enzyme activity. In contrast, $Ba^{++}$, $Hg^{++}$, $Pb^{++}$, $Ca^{++}$, $Mn^{++}$, $Cu^{++}$, $Fe^{+++}$, $Na^+$ and $K^+$ decreased it. The enzyme was inactivated by treatment with maleic anhydride, iodine and 2,4-dinitrophenol. The results indicate that active site is a imidazole group on the enzyme.

• Korean Journal of Microbiology
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• v.16 no.3
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• pp.122-130
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• 1978

During the sporulation stage in Saccharomyces cerevisiae J170, the incorporation of $D^{14}$ C-glucose into starved cells of sporulation stage as well as the vegetative one is appeared higher at pH 6.0. Glucose transport system, in both the vegetative and sporulation stage, is associated with "energy dependent" as the result of repression by such a respiratory inhibitor as 2, 4-dinitrophenol. The Km value of glucose uptake in vegetative stage and sporulation stage was 2.1 mM and 2.5 mM respectively, indicating that the glucose is considerably reuqired for vegetative growth. Competition and countertranspoer of glucose by frutose and galactose are more distinct in vegetative stage, comparing with sporulation stage. The main sugar components of yeast cells consists of ribose, mannose, and ${\alpha}, \;{\beta}-glucose$. Amounts of mannose is lower in the aporulation stage than that in the vegetative stage.

• Korean Journal of Microbiology
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• v.9 no.1
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• pp.39-45
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• 1971

During the sporulation stage in Saccharomyces cerevisiae J170, the incorporation of D$^{14}$ C-glucose into starved cells of sporulation stage as well as the vegetative one is appeared higher at pH 6.0. Glucose transport system, in both the vegetative and sporulation stage, is associated with "energy dependent" as the result of repression by such a respiratory inhibitor as 2,4-dinitrophenol. The Km value of glucose uptake in vegetative stage and sporulation stage was 2.1 mM and 2.5 mM respectively, indicating that the glucose is considerably reuqired for vegetative growth. Competition and countertranspoer of glucose by frutose and galactose are more distinct in vegetative stage, comparing with sporulation stage. The main sugar components of yeast cells consists of ribose, mannose, and .apha., .betha.-glucose. Amounts of mannose is lower in the aporulation stage than that in the vegetative stage.ive stage.

• Microbiology and Biotechnology Letters
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• v.20 no.3
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• pp.295-301
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• 1992

An alkaline protease producing microorganism was isolated from soil and identified as Streptomyces griseus HC-1141. The optimum pH and temperature for the purified enzyme activity were 8.0 and $60^{\circ}C$, respectively. The enzyme was relatively stable in the pH range of 7.0-9.0 and at the temperature below $60^{\circ}C$. The activity of purified enzyme was inhibited by $Hg^{2+}$, $Cu^{2+}$, $Zn^{2+}$, $Ba^{2+}$ and $Fe^{2+}$, whereas activated by $Mn^{2+}$ and $Ca^{2+}$. $\varepsilon$-Amino caproic acid, 2,4-dinitrophenol and iodine did not show inhibitory effect on the activity of alkaline protease, but p-chloromercuribenzoic acid, ethylendiaminetetraacetic acid showed inhibitory effect on the enzyme activity. These result suggested that the protease was metalloenzyme, and require a reactive SH group for the activity. The reaction of this enzyme follows typical Michaelis-Menten kinetics with the $K_m$ value of $2.229{\times}10^{-4}$M and the $V_{max}$ of $46.08 {\mu}$g/min for casein. The activation energy for the alkaline protease calculated by Arrhenius equation was 3.643 kcal/mol. This enzyme hydrolyzed casein more rapidly than the hemoglobin and egg albumin.

• Korean Journal of Microbiology
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• v.16 no.4
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• pp.148-154
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• 1978

Saccharomyces cerevisiae J170, a mutant, was used for $DL-^{14}C-leucine$ uptake during the sporulation and vegetative stage. $^{14}C-Leucine$ uptake into yeast cells appeared the highest at pH 6.0, indicating the same result of glucose transport, $^{14}C-Leucine$ uptake in sporulation period was higher than in growth phase, showing the evidence that leucine is more required for protein synthesis. This tendency has the evidence tht leucine is more required for protein synthesis. This tendency has the evidence that leucine is more required for protein synthesis. This tendency has been also supported from the result of Km values of leucine uptake in two stages of yeast. Leucine uptake was inhibited by 2,4-dinitrophenol in two stages of yeast. This means that leucine transport system is associated with energy dependent in both stages. The contents of all amino acid in growth phase cells were higher than those of sporulation stge cells, and those of methionine and tyrosine were showed in trace during the sporulation stage. In contrast, the content of glutamic acid in sporulation stage was compared with those of other amino acids.

• Microbiology and Biotechnology Letters
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• v.10 no.1
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• pp.1-7
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• 1982

A Rhizopus sp. was selected for its strong cellulolytic activity among various strains of molds found in rotting ginseng roots. Studies were made on some properties of the cellyloiytic enzyme produced by the strain. The results obtained were summarized as follows: The optimum pH of the enzyme was 4.5 and the range of its stability to the pH was 3.0 to 7.0. The optimum temperature was 5$0^{\circ}C$, while the enzyme was instantly inactivated above 6$0^{\circ}C$. Mn$^{＋＋}$ and Co$^{＋＋}$ ions increased enzyme activity and the metal ions were found to increased the ther-mostability of the enzyme. This enzyme was inhibited by sodium dodecyl sulfate and 2,4-dinitrophenol. This enzyme had a strong cellulolytic enzyme activity on various native cellulose given a sufficient reaction time. The addition of 0.5% saponin solution into reaction mixture increased the enzyme activity.

• Korean Journal of Environmental Agriculture
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• v.3 no.2
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• pp.16-22
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• 1984

This study was carried out to investigate the stability of dinobuton (2-sec-butyl-4,6-dinitrophenyl isopropyl carbonate) in distilled water and buffer solutions and its persistence in soils. When dinobuton was incubated at $30^{\circ}C$ and $60^{\circ}C$ in distilled water, the half-lives of dinobuton was 28 and 6 days, respectively. The decomposition of dinobuton was, therefore, faster at high temperature than at low temperature. The half-life of dinobuton was about 27 days in the acidic solution $(pH\; 4{\sim}6)$, whereas 10 and 4 days in the alkaline solutions of pH 9, and 10, respectively. Thus dinobuton was stable in acidic solution, and unstable in alkaline solution. Dinoseb (2-sec-butyl-4,6-dinitrophenol), which is produced in the degradation process of dinobuton, was produced in small amounts in distilled water and buffer solutions. The half-life of dinobuton in sterilized soil was about 16 days longer than in non-sterilized soil. Dinoseb was also more persistent in sterilized soil than in non-sterilized one.