• Journal of Korean Society of Environmental Engineers
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• v.38 no.5
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• pp.228-235
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• 2016

Nitrite accumulation is essential for constructing an anammox process. As the pH in the reactor exerts a complicated and strong influence on the reaction rate, we investigated its effects upon treatment of an ammonic wastewater (2,000 mgN/L) through modeling and experiment. The modeling results indicated that the reaction stability is strongly affected by pH, which results in a severe reduction of the 'stable region' of operation under alkaline environments. On a coordinate of the total ammonia nitrogen (TAN) concentration vs. pH, the maximal stable reaction rates and the maximal nitrite accumulation potentials could be found on the 'stability ridge' that separates the stable region from the unstable region. We achieved a stable and high ammonia oxidation rate (${\sim}6kgN/m^3-d$) with a nitrite accumulation ratio of ~99% when operated near the 'stability ridge'. The optimum pH that can be observed in experiments varies with the TAN concentrations utilized, although the intrinsic optimum pH is fixed. The direction of change is that the optimum operational pH falls as the TAN concentration increases, which is in excellent accordance with the observations in the literature. The optimum operational pH for 95% nitritation was predicted to be ~8.0, whereas it was ~7.2 for 55% partial nitritation to produce an anammox feed in our experimental conditions.

• Bulletin of the Korean Chemical Society
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• v.19 no.6
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• pp.645-649
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• 1998

In order to develop pH-sensitive liposomes that are stable in plasma, liposomes containing membrane-spanning bipolar amphiphiles as protonatable components were studied. Sonicated small unilamellar liposomes composed of dioleoylphosphatidylethanol amine (DOPE), dioleoylphosphatidylcholine (DOPC) and bis(6-hemisuccinyloxyhexyl) fumarate (BHF) in a 3 : 1 : 1 molar ratio are stable at neutral pH, but destabilized at weakly acidic pH with 50% leakage of entrapped materials at about pH 5.5. The liposomes are relatively stable in plasma such that only a few percent entrapped calcein was released in 50% plasma within 1.5 h incubation at 37 ℃, while about 10% entrapped calcein was released from sonicated liposomes composed of DOPE, DOPC, and oleic acid (OA) in a 3 : 1 : 1 molar ratio under the identical conditions. The aqueous contents mixing and lipid components mixing experiments suggest that the protonation of BHF may induce fusion between the liposomes, followed by the release of the entrapped materials.

• The Korean Journal of Mycology
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• v.17 no.3
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• pp.149-153
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• 1989

One strain of Aspergillus niger K-25 producing an acid-stable ${\alpha}-amylase$ was isolated from the soil. The optimum culture conditions were investigated. The production of the acid-stable ${\alpha}-amylase$ was enhanced when the strain was incubated in a medium containing soluble starch 3.5%, peptone 2%, $KH_2PO_4$ 0.5%, $MaSO_4{\cdot}7H_2O$ 0.25% and $FeCI_3$ 1.0% at pH 3 for 7 days. However, higher activity of acid-stable ${\alpha}-amylase$ was demonstrated on wheat bran culture. Amylase production was doubled when A. niger K-25 was incubated on the wheat bran supplemented with fumaric acid buffer (pH 3).

• The Korean Journal of Mycology
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• v.17 no.3
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• pp.145-148
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• 1989

An acid-stable ${\alpha}-amylase$ produced by Aspergillus niger K-25 strain was purified by fractional precipitation with ammonium sulfate, ethacridine and acetone. The final preparation was homogeneous in cellulose acetate electrophoresis. The enzyme retained 91 % of its oringinal activity at pH 3.0, 8.7% at pH 2.4. The optimum pH of the enzyme was around pH 4. The purified-enzyme with optimum temperature of $40^{\circ}C$ was more heat-stable than the commercial product. The enzyme retained 80% of its original activity when heated to $60^{\circ}C$ for 30 minutes while the commercial amylase lost its acitivity completely within 30 minutes at $50^{\circ}C$.

• Journal of the Korean Ceramic Society
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• v.32 no.10
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• pp.1123-1130
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• 1995

In the preparation of manganese zinc ferrite powders by alcoholic dehydration of citrate/formate solution. The effect of pH change on precipitation was investigated. The pH range for obtaining stable precipitates was studied. The glassy phase was obtained when the pH value of solution is higher than 5, and the formation mechanism of glassy phase was suggested. Below pH 5, the stable precipitates were formed, and the optimal pH was 2. Formation of glassy phase was accounted for the change of surface charge by pH change. The change of surface charge is caused by the interparticular agglomeration. The precipitate was redissolved into the water on the surface of precipitate itself and through the polymerization, it agglomerated. This mechanism is tought to be similar to that of viscous flow.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.4-10
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• 2005

Periodate-oxidized soluble starch increased pH stability of Aspergillus awamori a-glucosidase. After incubation for two hours, the enzyme in the absence of oxidized soluble starch was stable in the range of pH 3-7 at 40℃, pH 3-6 at 50℃ and the enzyme in the presence of oxidized soluble starch was stable in the range of pH 3-9 at 40℃, pH 3-8 at 50℃. At 60℃, the enzyme was stable in pH 3-6 regardless of the presence or absence of IO₄-oxidized soluble starch, but when IO₄-oxidized soluble starch existed in pH 5-6, remained activity of the enzyme increased 20% more than when it didn't exist. The enzyme modified with IO₄-oxidized soluble starch remained 70% of activity in pH 9, but native enzyme didn't remain, showing the increase of stability due to modification. In thermal stability, modified enzyme remained 12% at 50℃ and 7% at 80℃. But native enzyme remained 8% at 50℃ and didn't remain at more than 70℃. The result of HPLC analysis revealed the subunit of the enzyme at under pH 2 or over pH 9 was separated or the enzyme was denatured and conjugated. Protein structure of native enzyme was denatured by acidic and basic pH but was stable in the presence of IO₄-oxidized soluble starch.

• The Korean Journal of Food And Nutrition
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• v.13 no.4
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• pp.383-389
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• 2000

Stabilities to heat, pH, light were investigated about isolated red color pigment from the Korean Lithospermum erythrorhizon. The extracted pigment, acetylshikonin was stable heating at 40∼80$\^{C}$ for 1∼2 hours, hut it was specially unstable on the storage above 55$\^{C}$. The extracted pigment, acetylshikonin was stable on the sunlight under the red and green filters but unstable under the yellow and blue filters. The extracted pigment, acetylshikonin was stable under the pH of 4∼8 but unstable under the pH above 10. The extracted pigment, acetylshikonin was stable under the KCl and NaCl at concentration of 10$\^$-1/Mole. The pigment was very unstable under the CaCl$_2$, FeCl$_3$, CoCl$_2$, AlCl$_3$ and MnCl$_2$ at concentration of 10$\^$-1/Mole. The red pigment, acetylshikonin was stable under citric acid and acetic acid at concentration of 1 Mole. Especially, acetic acid was effective for the stability of the pigment.

• Korean journal of food and cookery science
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• v.12 no.1
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• pp.54-59
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• 1996

Immunoglobulins (IgY) were isolated from egg yolk of hens immunized with bovine serum albumin(BSA). The stability of anti-BSA IgY against heat and pH was investigated. Antibody activity was measured by enzyme linked immunosorbent assay. IgY was relatively heat-stable and most of the antibody activity remained after heating up 65$^{\circ}C$ for 30 minutes. IgY was stable at pH 5-11. However, inactivation of IgY was observed below pH 4, or above pH 12. Inactivation of IgY proceeded rapidly at low pHs(pH 2-3). Most of the antigen binding activity was lost at low pHs probably because of some conformational changes.

• YAKHAK HOEJI
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• v.39 no.1
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• pp.24-30
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• 1995

Lectin from mistletoe(Viscum coloratum) fermented by Lactobacillus plantarum was compared with the lectin from unfermented mistletoe. Agglunating activity of fermented mistletoe was stable at pH 3.77~8.71, at temperature range of $0~40^{\circ}C$ and in the presence of 9 mental ions, which results are similar to unfermented one, but less stable at pH 2.03~3.00 and more stable at temperature $60~80^{\circ}C$ than lectin from unfermented one. Agglunating activity of lectin from mistletoe fermented for 1 or 2 days and from fraction number 42~54 was not inhibited by all sugars used except for lectin from fraction number 21~34. Mitogenic activity to murine lymphpocytes of lectin from mistletoe was decreased by fermentation process.

• Journal of the Korean Mathematical Society
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• v.43 no.4
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• pp.783-801
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• 2006

Let A be the mod p Steenrod algebra for p an arbitrary odd prime and S the sphere spectrum localized at p. In this paper, some useful propositions about the May spectral sequence are first given, and then, two new nontrivial homotopy elements ${\alpha}_1{\jmath}{\xi}_n\;(p{\geq}5,n\;{\geq}\;3)\;and\;{\gamma}_s{\alpha}_1{\jmath}{\xi}_n\;(p\;{\geq}\;7,\;n\;{\geq}\;4)$ are detected in the stable homotopy groups of spheres, where ${\xi}_n\;{\in}\;{\pi}_{p^nq+pq-2}M$ is obtained in [2]. The new ones are of degree 2(p - 1)($p^n+p+1$) - 4 and 2(p - 1)($p^n+sp^2$ + sp + (s - 1)) - 7 and are represented up to nonzero scalar by $b_0h_0h_n,\;b_0h_0h_n\tilde{\gamma}_s\;{\neq}\;0\;{\in}\;Ext^{*,*}_A^(Z_p,\;Z_p)$ in the Adams spectral sequence respectively, where $3\;{\leq}\;s\;<\;p-2$.