• Journal of the Korean Electrochemical Society
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• v.18 no.2
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• pp.45-50
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• 2015

In the present work, to increase the chemical stability of the lithium-ion-conducting ceramic electrolyte ($Li_{1+x+y}Al_xTi_{2-x}Si_yP_{3-y}O_{12}$, LATP) in the strong alkaline solution, the surface of LATP was modified by the nitridation process. The surface and structural properties of nitride LATP solid electrolyte were characterized by X-ray diffraction, X-ray photoelectron spectrometer and scanning electron microscopy and ac-impedance spectroscopy, which were correlated to the chemical stability and electrochemical performance of LATP. The nitrided LATP immersed in the alkaline solution for 30 days exhibits the enhanced chemical stability than the pristine LATP. Moreover, a rechargeable hybrid Li-air battery constructed with the nitrided LATP solid electrolyte shows considerably reduced discharge-charge voltage gaps (enhanced the round-trip efficiency) in comparison to the cell constructed with pristine LATP, which indicate that the surface nitridation process can be the efficient way to improve the chemical stability of solid electrolyte in alkaline media.

• Journal of Microbiology and Biotechnology
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• v.21 no.12
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• pp.1250-1256
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• 2011

In this study, Bacillus licheniformis cells were immobilized by entrapment in calcium alginate beads and were used for production of alkaline protease by repeated batch process. In order to increase the stability of the beads, the immobilization procedure was optimized by statistical full factorial method, by which three factors including alginate type, calcium chloride concentration, and agitation speed were studied. Optimization of the enzyme production medium, by the Taguchi method, was also studied. The obtained results showed that optimization of the cell immobilization procedure and medium constituents significantly enhanced the production of alkaline protease. In comparison with the free-cell culture in pre-optimized medium, about 7.3-fold higher productivity was resulted after optimization of the overall procedure. Repeated batch mode of operation, using optimized conditions, resulted in continuous production of the alkaline protease for 13 batches in 19 days.

• Archives of Pharmacal Research
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• v.20 no.6
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• pp.643-646
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• 1997

Thermal stability of a red pigment, carthamin, frm Carthamus tinctorius was investigated to explore possible applications as natural color additives for foods, cosmetics, and nutraceuticals. Degree of degradation reactions of carthamin at acidic, neutral and alkaline conditions were determined with UV/V is spectral measurements. Decomposition half lives of carthamin at 25.deg. C were 4.0 h, 5.1 h, and 12.5 h at pH 5.0, pH 7.0, and pH 12.0, respectively, indicating that carthamin is much more stable at alkaline pH than acidic or neutral conditions. The activation energies of carthamin at pH 5.0, pH 7.0, and pH 12.0 were 15.6, 15.7 and 16.8 kcal/mol, respectively.

• Journal of environmental and Sanitary engineering
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• v.23 no.1
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• pp.25-31
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• 2008

A bacterial strain, Bacillus megaterium L-49 has been isolated and identified that produces alkaline ${\alpha}$-amylase. The cell is ellipsoidal, about $1.0-1.2{\times}3.0-3.6{\mu}m$ in diameter, Gram-positive, motile, and central partial central. Growth occurs in media containing 7% of NaCl. This strain could utilize D-glucose, lactose, xylose, sucrose, mannose, and maltose, and but it does not utilize D-fructose, and glycogen. Among the various concentrations of saturated ammonium sulfate, the retractation ratio in range of 70 to 100% was about 93%. However, in the case of acetone, it was about 98.7%. EDTA has activating effect and Ca2+ has no effect on alkaline ${\alpha}$-amylase activity. The alkaline ${\alpha}$-amylase has low thermal stability. The optimal temperature for reaction is $50^{\circ}C$. The alkaline ${\alpha}$-amylase activity maintained stabilizing at pH 6-11 and the optimal pH for reaction was 9-10.

• Korean Journal of Poultry Science
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• v.17 no.2
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• pp.127-133
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• 1990

This study was undertaken to find out the effect of heating time and temperature, pH and NaCl concentration on the heat stability of egg albumen gel during heat treatment. With the transient decrease at 110-$130^{\circ}C$, hardness of heat-set albumen gel was increased as the heating temperature increased. The cohesiveness showed similar trend as well. The lightness was decreased while the yellowness was increased as the heating time and temperature increased. Heat-set albumen gel showed maximum hardness at pH 4.5-5.0 and pH 9.0 High heat treatment($120^{\circ}C$, 30min) showed higher hardness at alkaline range compared to low heat treatment($96^{\circ}C$, 30min.). Color of the albumen gel was relatively dark at acidic range and bright at alkaline range. High heat treatment caused darker albumen gel at alkaline range and brighter albumen gel at acidic range. The addition of NaCl increased hardness and cohesiveness of the albumen gel and improved the lightness after high heat treatment regardless of NaCl concentration.

• KSBB Journal
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• v.27 no.6
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• pp.352-360
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• 2012

Bacillus clausii I-52 which produced SDS- and $H_2O_2$-tolerant extracellular alkaline protease (BCAP) was isolated from heavily polluted tidal mud flat of West Sea in Incheon, Korea and stable strain (transformant C5) of B. clausii I-52 harboring another copy of BCAP gene in the chromosome was developed using the chromosome integration vector, pHPS9-fuBCAP. When investigated the production of BCAP using B. clausii transformant C5 through pilot-scale submerged fermentation (500 L) at $37^{\circ}C$ for 30 h with an aeration rate of 1 vvm and agitation rate of 250 rpm, protease yield of approximately 105,700 U/mL was achieved using an optimized medium (soybean meal 2%, wheat flour 1%, sodium citrate 0.5%, $K_2HPO_4$ 0.4%, $Na_2HPO_4$ 0.1%, NaCl 0.4%, $MgSO_4{\cdot}7H_2O$ 0.01%, $FeSO_4{\cdot}7H_2O$ 0.05%, liquid maltose 2.5%, $Na_2CO_3$ 0.6%). The enzyme stability of BCAP was increased by addition of polyols (10%, v/v) and also, the stabilities of BCAP towards not only the thermal-induced inactivation at $50^{\circ}C$ but also the SDS and $H_2O_2$-induced inactivation at $50^{\circ}C$ were enhanced. Among the polyols examined, the best result was obtained with propylene glycol (10%, v/v). The BCAP supplemented with propylene glycol exhibited extreme stability against not only the detergent components such as ${\alpha}$-orephin sulfonate (AOS) and zeolite but also the commercial detergent preparations. The granulized enzyme of BCAP was prepared with approximately 1,310,000 U/g of granule. Wash performance analysis using EMPA test fabrics revealed that BCAP granule exhibited high efficiency for removal of protein stains in the presence of anionic surfactants as well as bleaching agents. When compared to Savinase 6T$^{(R)}$ and Everlase 6T$^{(R)}$ manufactured by Novozymes, BCAP under this study probably showed similar or higher efficiency for the removal of protein stains. These results suggest that the alkaline protease produced from B. clausii transformant C5 showing high stability against detergents and high wash performance has significant potential and a promising candidate for use as a detergent additive.

• Analytical Science and Technology
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• v.6 no.5
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• pp.471-477
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• 1993

The novel macrocylic ligand {(4, 5):(13, 14)-dibenzo-6, 9, 12-trioxa-3, 15, 21, -triazabicyclo [15. 3. 1]heneicosa-(1, 17, 19)(18, 20, 21) triene: HDBPDA} was synthesized, and protonable constants of the ligand and the complex stability constants with alkali metals alkaline earth metals were determined. We evaluated the resolution factor(${\Delta}$) from equation that inducing from stability constants(pK). Also, this ligand was grafted on chloromethylated styrene-divinyl benzene(Merrifield resin) for HDBPDA, ion exchanger. Alkali and alkaline earth metal ions were separated using water by the column chromatography with this ion exchanger. Selectivity(${\alpha}$) and resolution(Rs) of alkali and alkaline earth metal ions were measured from the elution curves chromatogram. The selectivity and resolution values of the various ions calculated from the elution curves were compared with those abtained from pK values. The results were in a good agreement between tow methods. Ion exchange capacity of the resin were determined using the alkali and alkaline earth metal ions and pH dependence of capacity was also discussed.

• Membrane Journal
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• v.31 no.4
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• pp.275-281
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• 2021

To evaluate the possibility as a separator in alkaline water electrolysis, the thermal stability, ion conductivity and durability of 5 commercially available anion exchange membranes were tested. The thermal stability of FAAM-PK-75 and FAAM-40 membrane analyzed by thermo-gravimetric analysis (TGA) showed good performance compared to the other three types of AEM, AHO, and AHA membrane. The ion conductivity of AEM membrane measured in 7 M KOH solution at 25℃ and 80℃ had a higher value of about 4~17 times compared to the other membranes. The durability of FAAM-PK-75 tested in 7 M KOH solution at 25℃ was high compared to the other membranes.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.290-296
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• 1998

Interspecific hybrids between Aspergillus oryzae var. oryzae and Penicillium chrysogenum (Tyr$\^$-/), high alkaline protease producing fungi, were obtained by nuclear transfer technique. Nuclei isolated from the wild type Aspergillus oryzae var. oryzae strain were transferred into auxotrophic Penicillium chrysogenum mutants and selected the new strains showing an increased protein degrading capability. Maximum production of protoplasts were obtained by 1% Novozym 234 at $30^{\circ}C$ for 3 hours and the most effective osmotic stabilizers for the isolation of protoplasts were 0.6M KCl. Frequencies of hybrid formation by nuclear transfer were 1.3${\times}$10$\^$-3/∼2.8${\times}$10$\^$-3/. They could be suggested as an aneuploid by the observation of genetic stability, conidial size, DNA content, and nuclear strain. The hybrids showed 1.1～2.2 fold higher alkaline pretense activities than parental strains.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.427-434
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• 1998

An alkaline protease was 4-fold purified, yielding 2.3% of recovery by ammonium sulfate precipitation, CM-cellulose column chromatography and Sephadex G-100 column chromatography. The purified enzyme was estimated to be monomeric with molecular weight of about 62,000 from polyacrylamide gel eletrophoresis (PAGE) and sodiumdodecylsulfate polyacrylamide gel electrophoresis (SDS-FAGE). The optimal pH and temperature of the alkaline pretense activity were 11.0 and 50$^{\circ}C$, respectively, exhibiting high stability at pH value from 6.0 to 11.0 at 50$^{\circ}C$ for 30 minute. The alkaline pretense was activated by MnSO$_4$, CaCl$_2$, and was inhibited by CuSO$_4$, ZnSO$_4$, HgCl$_2$, EDTA and EGTA. Also, the enzyme was found to be a metaloenzyme requiring Mn$\^$2+/ as cofactor. The NH$_2$-terminal amino acid of alkaline protease was alanine. The Km and Vmax values of this enzyme for casein was 4.0 mg/$m\ell$ and 5,500 unit/$m\ell$, respectively.