• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.338-338
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• 2005

• Journal of Pharmaceutical Investigation
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• v.26 no.4
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• pp.309-314
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• 1996

The purpose of this study is to explain the relationship between the pharmacological mechanism of levamisole and the cellular activity of cellular alkaline phosphatase (ALPase) in kidney cells. The results of our investigation were as follows. 1. Cellular ALPase activity in Macacus rhesus monkey kidney cells (MA 104 cells) and primary cultured rabbit kidney proximal tubular cells treated with levamisole was increased about two or three times than control. However, 50% of ALPase activity in cultured medium was inhibited by levamisole itself. 2. The proliferation of MA 104 and cultured rabbit kidney proximal tubular cells was linearly decreased in paralleled with increase of levamisole concentration $(50\;and\;500\;{mu}M)$ with MTT test. 3. In the heat stability tests, the inhibition of ALPase activity with and without levamisole at $56^{\circ}C$ in MA 104 cells showed different $IC_{50}$ values. 4. HPLC analysis of levamisole metabolites produced by cultured MA 104 cells suggested that the formation of a metabolite, that may be associated with its increase of cellular ALPase activity. Based on these results, we assumed that the increase of cellular ALPase activity by levamisole was evoked by modification of the ALPase catalytic sites.

• Journal of the Korean Chemical Society
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• v.27 no.3
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• pp.208-212
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• 1983

The stability constants for the complexes formed between dibenzo-18-crown-6 compound and alkaline earth metal cations in dimethylsulfoxide, dimethylformamide, and acetonitrile have been obtained by conductometry at $25{\circ}C\;and\;35{\circ}C$respectively. The stability constants were increased in order of $Ca^{2+} in any solvent, and the magnitudes were found to be reversely proportional to the solvent donicities. The result could be understood in terms of ion-cavity radius concept, solvent basicity, and solvation of the cations.

• Journal of Hydrogen and New Energy
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• v.29 no.5
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• pp.458-465
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• 2018

This study reports the fabrication of anion exchange membranes (AEMs) containing two kinds of functional groups: i) trimethylphosphite (TMP) and ii) trimethylamine (TMA). We carried out the synthesis of polymers to enhance thermal stability and ion conductivity. The alternative polymer was prepared using 2,2-bis(4-hydroxy-3-methylphenyl)propane and decafluorobiphenyl. The membrane was fabricated by solution casting method. The thermal stability of membranes was examined by TGA. The physiochemical properties of membranes were also investigated in terms of water uptake, swelling ratio, ion exchange capacity, and ion conductivity. The hydroxide ion conductivity of the membranes reached about 20.2 mS/cm for quaternary ammonium poly(arylene ether) (QA-PAE) containing TMA moiety and 5.1 mS/cm for quaternary phosphonium PAE (QP-PAE) containing TMP moiety at $90^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.25 no.6
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• pp.845-855
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• 2015

The present study describes the gene cloning and high-level expression of an alkaline and thermostable lipase gene from Trichosporon coremiiforme V3. Nucleotide analysis revealed that this lipase gene has an open reading frame of 1,692 bp without any introns, encoding a protein of 563 amino acid residues. The lipase gene without its signal sequence was cloned into plasmid pPICZαA and overexpressed in Pichia pastoris X33. The maximum lipase activity of recombinant lipase was 5,000 U/ml, which was obtained in fed-batch cultivation after 168 h induction with methanol in a 50 L bioreactor. The purified lipase showed high temperature tolerance, and being stable at 60℃ and kept 45% enzyme activity after 1 h incubation at 70℃. The stability, effects of metal ions and other reagents were also determined. The chain length specificity of the recombinant lipase showed high activity toward triolein (C18:1) and tripalmitin (C16:0).

• Membrane Journal
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• v.31 no.6
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• pp.371-383
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• 2021

Anion exchange membranes have been used for water electrolysis, which can produce hydrogen, and fuel cells, which can generate electrical energy using hydrogen fuel. Anion exchange membranes operate based on hydroxide ion (OH^-) conduction under alkaline conditions. However, since the anion exchange membrane shows relatively low ion conductivity and alkaline stability, there is still a limit to its commercialization in water electrolysis and fuel cells. To address these issues, it is important to develop novel anion exchange membrane materials by rationally designing a polymer structure. In particular, the polymer structure and synthetic method need to be controlled. By doing so, for polymers, the physical properties, ionic conductivity, and alkaline stability can be maintained. Among many anion exchange membranes, poly(2,6-dimethyl-1,4-phenylene oxide) (PPO) is commercially available and easily accessible. In addition, the PPO has relatively high mechanical and chemical stability compared to other polymers. In this review, we introduce the recent development strategy and characteristics of PPO-based polymer materials used in anion exchange membranes.

• Journal of Microbiology and Biotechnology
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• v.25 no.5
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• pp.662-671
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• 2015

To enrich the genetic resource of microbial xylanases with high activity and stability under alkaline conditions, a xylanase gene (xynSL4) was cloned from Planococcus sp. SL4, an alkaline xylanase-producing strain isolated from the sediment of soda lake Dabusu. Deduced XynSL4 consists of a putative signal peptide of 29 residues and a catalytic domain (30-380 residues) of glycosyl hydrolase family 10, and shares the highest identity of 77% with a hypothetical protein from Planomicrobium glaciei CHR43. Phylogenetic analysis indicated that deduced XynSL4 is closely related with thermophilic and alkaline xylanases from Geobacillus and Bacillus species. The gene xynSL4 was expressed heterologously in Escherichia coli and the recombinant enzyme showed some superior properties. Purified recombinant XynSL4 (rXynSL4) was highly active and stable over the neutral and alkaline pH range from 6 to 11, with maximum activity at pH 7 and more than 60% activity at pH 11. It had an apparent temperature optimum of 70℃ and retained stable at this temperature in the presence of substrate. rXynSL4 was highly halotolerant, retaining more than 55% activity with 0.25-3.0 M NaCl and was stable at the concentration of NaCl up to 4M. The enzyme activity was significantly enhanced by β-mercaptoethanol and Ca²⁺ but strongly inhibited by heavy-metal ions and SDS. This thermophilic and alkaline- and salt-tolerant enzyme has great potential for basic research and industrial applications.

• Membrane and Water Treatment
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• v.7 no.5
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• pp.417-431
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• 2016

Poly(vinylidene fluoride) (PVDF) powder was treated with aqueous sodium hydroxide to obtain partially defluorinated fluoropolymers with expected properties such as improving hydrophilicity and fouling resistance. Raman spectrum and FT-IR results confirmed the existence of conjugated carbon double bonds after alkaline treatment. As the concentration increased, the degree of defluorination increased. The morphology and structure of membranes were examined. The permeation performance was investigated. The results showed that membrane's hydrophilicity increased with increase of the percentage of alkaline treated PVDF powder. Moreover, in terms of the water contact angle, it decreased from $92^{\circ}$ to a minimum of $68^{\circ}$; while water up take increased from 128 to 138%. Fluxof pure water and the cleaning efficiency increased with the increase of alkaline treated PVDF powder. The fouling potential also decreased with the increase of the percentage of alkaline treated PVDF powder. The reason that makes blending PVDF show different characteristics because of partial defluorination, which led the formation of conjugated C = C bonds and the inclusion of oxygen functionalities. The polyene structure followed by hydroxide attack to yield hydroxyl and carbonyl groups. Therefore, the hydrophilicity of blending membrane was improved. The SEM and porosity measurements showed that no obvious variations of the pore dimensions and structures for blend membranes were observed. Mechanical tests suggest that the high content of the alkaline treated PVDF result in membranes with less tolerance of tensile stress and higher brittleness. TGA results exhibited that the blend of alkaline treated PVDF did not change membrane thermal stability.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.358-364
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• 1989

A crystalline alkaline pretense- producing Streptomyce sp. YSA-130 was isolated from soil in alkaline medium(pH 10.5). The optimum culture condition of Streptomyce sp. YSA-130 for the production of alkaline protease was as follows; 2.0% soluble starch, 1.0% soytone, 0.3% $K_2$HPO$_4$, 0.02% MgSO$_4$.7$H_2O$, 0.8% Na$_2$CO$_3$, pH 10.5, 3$0^{\circ}C$, and 12 hr. The alkaline pretense from the culture broth of Streptomyce sp. YSA-130 was purified about 24 folds by ammonium sulfate precipitation , dialysis, DEAE-cellulose ion exchange chromatography, gel filtration on Sephadex G-15 and crystallization. Optimum temperature and pH of purified enzyme were 6$0^{\circ}C$, and 11.5. Temperature and pH stability of purified enzyme were 5$0^{\circ}C$, and 5.5-12.0. Calcium ion was effective to stabilize the enzyme at higher temperature. The molecular weight of the purified enzyme was approximately 30,000. The purified enzyme was inactivated by diisopropyl flurophosphate(DFP) but not affected by metal ion, EDTA, sulfhydryl reagent and stable detergent.

• Journal of Pharmaceutical Investigation
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• v.18 no.3
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• pp.125-131
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• 1988

This study was undertaken to investigate the proteolytic enzyme from Neungee mushroom [Sarcodon aspratus (Berk) S. Ito]. The proteolytic activity of Neungee was higher than other several edible mushrooms under various pHs. The potency of proteolytic enzyme of Neungee was same as the digestive drugs containing protease. So the proteolytic activity of the enzyme was increased in neutral or weak alkaline pH, whose characteristics would be alkaline protease. The specific activity of the purified enzyme obtained by using Tris acryl CM-cellulose ion exchange increased 20 times as compared with that of the crude extract. The proteolytic enzyme was stable at room temperature, but decomposition was fast when incubated at higher temperature more than $40^{\circ}C$. The half life of the enzyme was longest in neutral pH and rate constant was increased in acidic or alkaline solution.