• Nutrition Research and Practice
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• v.6 no.2
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• pp.97-105
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• 2012

$Schizandra$ $chinensis$ Baillon is a traditional folk medicine plant that is used to treat and prevent several inflammatory diseases and cancer in Korea, but the underlying mechanisms involved in its anti-allergic activity are not fully understood. This study was designed to investigate mechanisms of anti-allergic activity of a $Schizandra$ $chinensis$ Baillon water extract (SCWE) in immunoglobulin E (IgE)-antigen complex-stimulated RBL2H3 cells and to assess whether gastric and intestinal digestion affects the anti-allergic properties of SCWE. Oxidative stress is an important consequence of the allergic inflammatory response. The antioxidant activities of SCWE increased in a concentration-dependent manner. RBL-2H3 cells were sensitized with monoclonal anti-dinitrophenol (DNP) specific IgE, treated with SCWE, and challenged with the antigen DNP-human serum albumin. SCWE inhibited ${\beta}$-hexosaminidase release and expression of interleukin (IL)-4, IL-13, and tumor necrosis factor-alpha (TNF-${\alpha}$) mRNA and protein in IgE-antigen complex-stimulated RBL2H3 cells. We found that digested SCWE fully maintained its antioxidant activity and anti-allergic activity against the IgE-antigen complex-induced activation of RBL-2H3 cells. SCWE may be useful for preventing allergic diseases, such as asthma. Thus, SCWE could be used as a natural functional ingredient for allergic diseases in the food and/or pharmaceutical industries.

• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.580-586
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• 1989

Penicillium sp. CB-20 was selected for strong polygalacturonase activity among various strains of molds found in soil. The optimum pH for the enzyme activity was 5.0 and optimum temperature was 4$0^{\circ}C$. The enzyme was relatively stable in acidic condition and unstable by heat treatment. The activation energy, Km and V$_{max}$ for the polygalacturonase were 2.499 Kcal/mol, 2.13$\times$10$^{-2}$mol/l, and 104.17 $\mu$mol/min. The activity of polygalacturonase was inhibited by Ag$^{+}$, Cu$^{++}$, Pb$^{++}$, Fe$^{+++}$, $Ca^{++}$, Na$^+$, Mn$^{++}$. The enzyme can be inactivated by the treatment ethylenediamintetra acetic acid, 2,4-dinitrophenol and $H_2O$$_2$. The results indicate the possible involvement of histidine, chelate and terminal amino group as active site. The enzyme was endo-type polygalacturonase.

• The Korean Journal of Physiology
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• v.26 no.1
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• pp.55-68
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• 1992

The effects of changes in extracellular $Na^+\;and\;Ca^+$ concentration on the membrane potential and contractility were studied in the antral circular muscle of guinea pig stomach in order to elucidate the existence and the nature of $Na^+/Ca^{2+}$ exchange mechanism. All experiments were performed in tris buffered Tyrode solution which was aerated with 100% $O_2$ and kept at $35^{\circ}C.$ The treatment of $10^{-5}$ ouabain was performed to induce intracellular $Na^+$ loading prior to the start of experiment. The results were as follows: 1. $Na^+$-free Tyrode or high $Ca^{2+}$-Tyrode solution hyperpolarized the membrane potential and induced contracture. The time course of contracture was similar to that of change in membrane potential. 2. The degree of hyperpolarization and the amplitude of contracture decreased in accordance with the increase of extracellular $Na^+$ concentration. 3. $Na^+$-free contracture was developed even after blocking the influence of intrinsic nerves by the pretreatment with atropine, guanethidine and TTX. 4. $Ca^{2+}$-channel blockers(D-600 or $Mn^{2+}$) and the blocker of intracellular $Ca^{2+}$ release from sarcoplasmic reticulum(ryanodine) did not suppress the development of $Na^+$-free contracture. And also, dinitrophenol had no effect on $Na^+$-free contracture. 5. Dose-response relationship between extracellular $Na^+$ concentrations and the magnitude of contractures showed a sigmoid pattern. The slope of straight line from Hill plot was 2.7. 6. In parallel with the increase of extracellular $Ca^{2+}$ concentration, the amplitude of contracture increased dose dependently and was maximum at 8 mM $Ca^{2+}$-Tyrode solution. 7. The relationship between extracellular $Ca^{2+}$ concentrations and the magnitude of contractures showed hyperbolic pattern. The slope of straight line from Hill plot was 1.1. From the above results, it is suggested that $Na^+/Ca^{2+}$ exchange mechanism exists in the antral circular muscle of guinea pig stomach and this mechanism affects the membrane potential electrogenically.

• Journal of Microbiology and Biotechnology
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• v.15 no.2
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• pp.412-420
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• 2005

In order to investigate factors affecting the denitrification in the F-STEP PROCESS using a loess ball as support media and Pseudomonas DWC 17-8, calcining temperature, loess ball size, pH, nitrate concentration, working temperature, and inhibitor were studied in batch mode using synthetic sludge. A 5- 10 mm of loess ball (960$^{circ}$ of calcining temperature) was the most suitable for denitrification. When the initial pH was increased from 3.0 to 7.0, the removal efficiency of nitrate was increased. Specifically, at initial pH of 7.0, the maximum removal efficiency of nitrate was 5.0 mg/min. When the initial concentration of nitrate was increased from 100 to 400 mg/l, the removal efficiency of nitrate was proportional to the concentration of nitrate. The maximum removal efficiency of nitrate was 5.72 mg/min at 400 mg/l of initial concentration. When the operating temperature was increased from 10 to 30$^{circ}$, the removal efficiency of nitrate was increased from 0.76 to 6.15 mg/min, and at above 40$^{circ}$ of operating temperature, it was decreased from 4.0 to 2.0 mg/min. Among the various inhibitors, higher than 10$^{-1}$ M of sodium azide abolished this reaction completely. When the KCN concentration was above 10$^{-1}$ M, the reaction was inhibited completely. In the case of 2,4-dinitrophenol and sodium sulphide, it was inhibited at above 10$^{-2}$ M completely. For testing the various flow orders of the F-STEP PROCESS for effective denitrification using practical wastewater, continuous experiments under the optimum conditions were carried out for 60 days. Among the various processes, the PROCESS A gave the highest efficiencies of denitrification, nitrification, and total nitrogen (TN) removal with 86.5, 89.5, and $90\%$, respectively. For scale-up in the PROCESS A, real farm wastewater was used and pilot tests carried out for 90 days. The denitrification efficiency was $97.5\%$, which was increased by $12.7\%$. The efficiencies of TN removal and nitrification were 96.6 and $70.0\%$, respectively. The removal efficiency of chemical oxygen demand (COD) was $63.7\%$, which was increased by $20\%$.

• Korean Journal of Veterinary Research
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• v.40 no.2
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• pp.267-274
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• 2000

Since intracellular free $Mg^{2+}$ ($[Mg^{2+}]_i$) appears to be tightly regulated following cellular energy depletion, we hypothesized that the increase in $[Mg^{2+}]_i$ would result in $Mg^{2+}$ extrusion into circulation. Extracellualr $Mg^{2+}$ contents ($[Mg^{2+}]_o$) were measured in rat erythrocytes, the perfused heart and liver, and plasma in the anesthetized rat. Animals were injected intraperitoneally with sodium nitrite ($NaNO_2$) and plasma $Mg^{2+}$ was measured after the injection and then 10 and 20 minutes later. An increase in circulating (plasma) $Mg^{2+}$ ($[Mg^{2+}]_c$) and methemoglobin was observed in animals injected with $NaNO_2$ (30 mg/Kg). The time course of the effects demonstrated that $[Mg^{2+}]_c$ and methemoglobin continued to increase 10 minutes after the $NaNO_2$ injection. Under these conditions, there was a sustained increase in $[Mg^{2+}]_c$, but not in methemoglobin, which was inhibited by pretreatment with potassium cyanide (KCN, 4 mg/Kg), indicating that an increase in $[Mg^{2+}]_c$ was accompanied by ATP depletion. Injection of rotenone (0.9 mg/Kg) or 2,4-dinitrophenol (15 mg/Kg) also induced an increase in $[Mg^{2+}]_c$. Reduced respiration rate from 100/min to 10/min during 30 minutes also caused a time-dependent rise in $[Mg^{2+}]_c$. These increase in $[Mg^{2+}]_c$ were inhibited by pretreatment with KCN. In addition, ATP depletion by $NaNO_2$ or KCN sustainedly increased the $[Mg^{2+}]_o$ in rat erythrocytes. $Mg^{2+}$ efflux was stimulated by KCN in the perfused heart and liver, but not by $NaNO_2$. These results suggest that the activation of $Mg^{2+}$ effluxes into the circulation is directly dependent on the ATP depletion-induced increase in $[Mg^{2+}]_i$ and heart, liver and erythrocytes have a major pool of $Mg^{2+}$ that can be mobilized upon cellular energy state.

• Korean Journal of Food Science and Technology
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• v.32 no.5
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• pp.1158-1167
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• 2000

To produce ${\beta}-cyclodextrin({\beta}-CD)$, a cyclodextrin glucanotransferase(CGTase) producing Aspergillus sp. CC-2-1 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. It was found that production of CGTase reached to the maximum when the wheat bran medium containing 0.1% albumin, 2% $(NH_4)_2S_2O_8$, 2% soluble starch and 0.2% $KH_2PO_4$ was cultured for 5 days at $37^{\circ}C$. The purity of CGTase was increased by 13.14 folds after DEAE-cellulose ion exchange chromatography and Sephadex G-100, G-150 gel filtration and the specific activity was 172.14 unit/mg. Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. The molecular weight of CGTase was estimated to be 27,800 by Sephadex G-100 gel filtration and SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the CGTase activity were 9.0 and $80^{\circ}C$, respectively. The enzyme was stable in pH $8.0{\sim}11.0$ at $60{\sim}80^{\circ}C$. The activity of purified enzyme was activated by $K^+,\;Cu^{2+}$ and $Zn^{2+}$. The activity of the CGTase was inhibited by the treatment with 2,4-dinitrophenol and iodine. The result suggests that the purified enzyme has phenolic hydroxyl group of tyrosine, histidine imidazole group and terminal amino group at active site. The reaction of this enzyme followed typical Michaelis-Menten kinetics with the $K_m$ value of 18.182 g/L with the $V_{max}$ of 188.68 ${\mu}mole/min$. The activation energy for the CGTase was calculated by Arrhenius equation was 1.548 kcal/mol.