• Journal of Microbiology and Biotechnology
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• v.24 no.12
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• pp.1673-1678
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• 2014

The interactive inhibitory effects of pH and chloride on the catalysis of laccase from Trametes versicolor were investigated by studying the alteration of inhibition characteristics of sodium chloride at different pHs for the oxidation of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid). At pH 3.0, the addition of sodium chloride (50 mM) brought about a 40-fold increase in $K{_m}^{app}$ and a 4-fold decrease in $V_{max}{^{app}}$. As the pH increased to 7.0, the inhibitory effects of sodium chloride became significantly weakened. The mixed-inhibition mechanism was successfully used to quantitatively estimate the competitive and uncompetitive inhibition strengths by chloride at two different pHs (pH 3.0 and 6.0). At pH 3.0, the competitive inhibition constant, $K_i$, was 0.35 mM, whereas the uncompetitive inhibition constant, $K{_i}^{\prime}$, was 18.1 mM, indicating that the major cause of the laccase inhibition by chloride is due to the competitive inhibition step. At a higher pH of 6.0, where the inhibition of the laccase by hydroxide ions takes effect, the inhibition of the laccase by chloride diminished to a great extent, showing increased values of both the competitive inhibition constant ($K_i=23.7mM$) and uncompetitive inhibition constant ($K{_i}^{\prime}=324mM$). These kinetic results evidenced that the hydroxide anion and chloride share a common mechanism to inhibit the laccase activity.

• Journal of Korean Society of Industrial and Systems Engineering
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• v.37 no.3
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• pp.36-42
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• 2014

Domestic 105mm HE (High Explosive) shell is composed of three parts that are Fuze, Projectile and Propellants. Among three parts, propelling charge of propellants part consists of single base propellants. It has been known that the lifespan of single base propellants is affected by a storage period. These are because Nitrocellulose (NC) which is the main component of propelling gunpowder can be naturally decomposed to unstable substances similar with other nitric acid ester. Even though it cannot be prevented fundamentally from being disassembled, a decomposition product ($NO_2$, $NO_3$, and $HNO_3$) and tranquillizer DPA (Diphenylamine) having high reactivity are added into a propellant to restrain induction of automatic catalysis by a decomposition product. The decay rate of the tranquillizer is also affected by a production rate of the decomposition product of NC. Therefore, an accurate prediction of the Self-Life is required to ensure against risks such as explosion. Hereupon, this paper presents a new methodology to estimate the shelf-life of single base propellants using data of ASRP (Ammunition Stockpile Reliability Program) to domestic 105mm HE (propelling charge of propellants part). We selected four attributes that are inferred to have influence on distribution of the DPA amount in a propellant from the ASRP dataset through data mining processes. Then the selected attributes were used as independent variables in a regression analysis in order to estimate the shelf-life of single base propellants.

• Bulletin of the Korean Chemical Society
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• v.35 no.8
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• pp.2438-2442
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• 2014

A kinetic study is reported for $S_NAr$ reaction of 1-fluoro-2,4-dinitrobenzene (5a) and 1-chloro-2,4-dinitrobenzene (5b) with alkali-metal ethoxides (EtOM, M = Li, Na, K and 18-crown-6-ether complexed K) in anhydrous ethanol. The second-order rate constant increases in the order $k_{EtOLi}$ < $k_{EtO^-}$ < $k_{EtONa}$ < $k_{EtOK}$ < $k_{EtOK/18C6}$ for the reaction of 5a and $k_{EtOLi}$ < $k_{EtONa}$ < $k_{EtO^-$ < $k_{EtOK}$ < $k_{EtOK/18C6}$ for that of 5b. This indicates that $M^+$ ion behaves as a catalyst or an inhibitor depending on the size of $M^+$ ion and the nature of the leaving group ($F^-$ vs. $Cl^-$). Substrate 5a is more reactive than 5b, although the $F^-$ in 5a is ca. $10pK_a$ units more basic than the $Cl^-$ in 5b, indicating that the reaction proceeds through a Meisenheimer complex in which expulsion of the leaving group occurs after the rate-determining step (RDS). $M^+$ ion would catalyze the reaction by increasing either the nucleofugality of the leaving group through a four-membered cyclic transition state or the electrophilicity of the reaction center through a ${\pi}$-complex. However, the enhanced nucleofugality would be ineffective for the current reaction, since expulsion of the leaving group occurs after the RDS. Thus, it has been concluded that $M^+$ ion catalyzes the reaction by increasing the electrophilicity of the reaction center through a ${\pi}$-complex between $M^+$ ion and the ${\pi}$-electrons in the benzene ring.

• Applied Chemistry for Engineering
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• v.5 no.2
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• pp.295-304
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• 1994

$Mo-V-O/SnO_2$(VM/Sn) and $SnO_2/Mo-V-O$(Sn/VM) catalysts have been prepared and characterized by XRD, BET, SEM and TPD of ammonia. The catalytic reaction of acrolein oxidation with these catalysts, in a continuous-flow fixed-bed reactor, showed that they had higher conversion of acrolein and higher yield of acrylic acid than those of Mo-V-O itself. The origin of the observed synergy studied by TPD, TPR and TPO is explained by the cooperation of $SnO_2$ and Mo-V-O at their interfaces where electrons flow from Mo-V-O phase to $SnO_2$ and $SnO_2$ produces spill-over oxygens, which, by being transported onto the surface of Mo-V-O, reoxidize the partially reduced active sites.

• Archives of Pharmacal Research
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• v.22 no.5
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• pp.464-473
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• 1999

Regulation of phosphcholine-hydrolyzing phosphatase (phosphocholine-phosphatase) activity, purified from bovine brain, was examined under physiological conditions. Various endogenous phosphomonoesters, which were utilized as substrate, inhibited the phosphocoline-phosphatase activity competitively (Ki 5.5-$82.0 {\mu}M$); among phosphomonoesters tested, there was a similar order of capability between the binding affinity of substrate and the inhibitory potency. In addition, phosphate ions also inhibited the phosphatase activity competitively with a Ki value of approximately $16{\mu}M$. Although leucine or theophylline inhibited the phosphatase activity at pH 9.0, their inhibitory action decreased greatly at pH 7.4. The pH-Km and pH-Vm profiles indicate that ionizable amino acids are involved in substrate binding as well as catalysis, alluding that the phosphatase activity may be highly dependent on the intracellular pH. Amino acid modification study supports the existence of tyrosine, arginine or lysine residue in the active site, and the participation of tyrosine residue in the catalytic action may e suggested positively for the susceptibility to the action of tetranitromethane or HOl-generator. Separately, the oxidative inactivation of phosphocholine-phosphatase activity was investigated. Of oxidants tested, HOONO, HOCl, HOl and $ascorbate/Cu^{2+}$ system were effective to inactivate the phosphatase activity. Noteworthy, a remarkable inativation was accomplished by $30{\mu}M$ HOCl in combination with 1 mM Kl. Inaddition, $Cu^{2+}(3{\mu}M) $in combination with ascorbate at concentrations as low as 0.1-0.3 mM reduced the phosphatase activity to a great extent. From these results, it is proposed that the phosphocholine-phosphatase activity may be regulated endogenously and susceptible to the various oxidant system in vivo.

• Macromolecular Research
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• v.16 no.5
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• pp.429-433
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• 2008

Alginate/carboxymethyl scleroglucan (CMSG) hydrogels were suggested as a novel carrier for the controlled release of protein drugs. The drug release characteristics of alginate hydrogels were improved by CMSG addition. Scleroglucan (Sclg) was carboxymethylated using monochloroacetic acid in aqueous alkaline medium. Alginate/CMSG hydrogels were prepared by dropping the mixture solution of alginate/CMSG into calcium chloride solution. The swelling behaviors and drug release characteristics of the hydrogels were investigated in the buffers of pH 1.2 or 7.4. As the CMSG content increased in the hydrogels, the swelling ratio of the alginate/CMSG hydrogel increased rapidly in the buffer of pH 7.4. At pH 1.2, however, the swelling ratio significantly decreased compared to that at pH 7.4. According to in vitro release tests, only 15% of ovalbumin, investigated as a model protein drug, was released from the alginate/CMSG hydrogels at pH 1.2 within 6 h. At pH 7.4, however, the drug release significantly increased due to the rapid swelling of the hydrogels. The release and swelling behaviors of the hydrogels could be controlled by changing the CMSG content in the hydrogels. These results supported the use of alginate/CMSG hydrogels as a suitable carrier for the controlled release of protein drugs in a pH responsive manner.

• Journal of the Korean Applied Science and Technology
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• v.21 no.4
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• pp.345-351
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• 2004

Highly ordered pure-silica MCM-41 materials possessing well-defined morphology have been successfully prepared with surfactant used as a template. The fabrication of mesoporous silica has received considerable attention due to the need to develop more efficient materials' for catalysis, separations, and chemical sensing. The surface modified MCM-41 was used as anadsorbent for biomolecules. Silica-supported organic groups and DNA adsorption on surface modified MCM-41 were investigated by FT-IR and UV-Vis spectrometer, respectively. The use of MCM-41 as the modification of electrode surfaces were investigated electrochemical properties of metal mediators with biomolecules. The modified ITO electrodes increased peak currents for a redox process of $[Ru(bpy)_3]^{2+}$ relative to the bare electrode. The electrochemical detection of DNA by cyclic voltammetry when the current is saturated in the presence of the mediator appeared more sensitive due to a higher catalytic current on the MCM-41 supported electrodes modified by carboxylic acid functional groups. The carboxyl or amine groups on the surface of MCM-41 interact and react with the $-NH_2$ groups of guanine and backbone, respectively. Highly ordered mesoporous materials with organic groups could find applications as DNA sensors.

• Journal of the Korean Chemical Society
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• v.40 no.5
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• pp.357-364
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• 1996

Stereochemistries of acetoxy 1,3-oxathiolane 1 were determined by two methods. First, the structures of $\alpha$ isomer 7 and $\beta$ isomer 9 were confirmed by the difference of their conversion rates to dihydrooxathiin 2 under acid catalysis. When the acetoxy leaving group is located in trans relationship to sulfur, a isomer in which carboxanilide is less hindered sterically against the 1,3-oxathiolane ring is $\beta$ isomer 7, and the other isomer of which the reaction rate is slower than 7 is $\beta$ isomer 9. Second, in the deuterium reactions of diastereomeric sulfoxides, the isomers of which methine hydrogen is substituted to deuterium were cis isomers 15 and 17, and another isomers of which methyl hydrogen is substituted to deuterium were trans isomers 16 and 18. Substitution of either methine or methyl hydrogen to deuterium resulted from stereospecific ring opening followed by recyclization by [2,3] sigmatropic rearrangement.

• Bulletin of the Korean Chemical Society
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• v.30 no.6
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• pp.1360-1364
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• 2009

The bacterium Sphingomonas chungbukensis DJ77 produces the extracellular polysaccharide gellan in high yield. Gellan produced by this bacterium is widely used as a gelling agent, and the enzyme UDP-glucose pyrophosphorylase (UGP) is thought to play a key role in the gellan biosynthetic pathway. The UGP gene has been successfully cloned and over-expressed in E. coli. The expressed enzyme was purified with a molecular weight of approximately 32 kDa, as determined by a SDS-polyacrylamide gel, but the enzyme appears as ca. 63 kDa on a native gel, suggesting that the enzyme is present in a homodimer. Kinetic analysis of UDP-glucose for UGP indicates $K_m$ = 1.14 mM and $V_{max}$ = 10.09 mM/min/mg at pH 8.0, which was determined to be the optimal pH for UGP catalytic activity. Amino acid sequence alignment against other bacteria suggests that the UGP contains two conserved domains: An activator binding site and a glucose-1-phosphate binding site. Site-directed mutagenesis of Lys194, located within the glucose-1-phosphate binding site, indicates that substitution of the charge-reversible residue Asp for Lys194 dramatically impairs the UGP activity, supporting the hypothesis that Lys194 plays a critical role in the catalysis.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.529-533
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• 1999

In addition to catalyzing the synthesis of dextran from sucrose as a primary reaction, dextransucrase also catalyzes the transfer of glucose from sucrose to other carbohydrates that are present or are added to the reaction digest. We have synthesized new glucans having new structures and new characteristics, by transferring D-glucose of sucrose to $\alpha$-cellulose and by using the constitutive dextransucrase obtained from Leuconostoc mesenteroides B-742CBM. The final reaction products were composed of soluble- and insoluble-glucans. The yields of soluble- and insoluble-glucans were theoretically 21% $\pm$ 2.2 and 68% $\pm$ 5.1, respectively. The remainder of the reaction products was recovered as a mixture of olgiosaccharides that could not be precipitated by 67%(v/v) ethanol. Treating the modified glucans with endo-dextranase and/or cellulase, oligosaccharides were produced that were not formed from the hydrolysis of native cellulose or B-742CBM dextran. The modification of the cellulose was confirmed by methylation and acid hydrolysis of the soluble-and insoluble-glucan. Both (1->4) and(1->6) glycosidic linkages were found in both of the glucans.