• Corrosion Science and Technology
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• v.2 no.1
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• pp.41-46
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• 2003

Flow-Accelerated Corrosion behavior concerning both activation and mass transfer process of SA106 Gr.C steel was studied using rotating cylinder electrode in room temperature alkaline solution by DC and AC electrochemical techniques. Passive film was tanned from pH 9.8 by step oxidation of ferrous product into hydroxyl compound. Corrosion potential shifted slightly upward with rotating velocity through the diffusion of cathodic species. Corrosion current density increased with rotating velocity in pH 6.98, while it soon saturated from 1000 rpm at above pH 9.8. On the other hand the limiting current increased with rotating speed regardless of pH values. It seems that activation process, which represents formation of passive film on the bare metal surface, controls the entire corrosion kinetics

• Journal of Microbiology and Biotechnology
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• v.33 no.2
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• pp.195-202
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• 2023

Protease is a widely used enzyme particularly in the detergent industry. In this research, we aimed to isolate alkaline protease-producing bacteria for characterization as a laundry detergent additive. The screening of alkaline protease production was investigated on basal medium agar plus 1% skim milk at pH 11, with incubation at 30℃. The highest alkaline protease-producing bacterium was 6BS15-4 strain, identified as Bacillus gibsonii by 16S rRNA gene sequencing. While the optimum pH was 12.0, the strain was stable at pH range 7.0-12.0 when incubated at 45℃ for 60 min. The alkaline protease produced by B. gibsonii 6BS15-4 using dairy effluent was characterized. The optimum temperature was 60℃ and the enzyme was stable at 55℃ when incubated at pH 11.0 for 60 min. Metal ions K⁺, Mg²⁺, Cu²⁺, Na⁺, and Zn²⁺ exhibited a slightly stimulatory effect on enzyme activity. The enzyme retained over 80% of its activity in the presence of Ca²⁺, Ba²⁺, and Mn²⁺. Thiol reagent and ethylenediaminetetraacetic acid did not inhibit the enzyme activity, whereas phenylmethylsulfonyl fluoride significantly inhibited the protease activity. The alkaline protease from B. gibsonii 6BS15-4 demonstrated efficiency in blood stain removal and could therefore be used as a detergent additive, with potential for various other industrial applications.

• Journal of the Institute of Electronics and Information Engineers
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• v.52 no.3
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• pp.199-205
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• 2015

This study is about ionic water generator filter Recently, a lot of people feel deep interest in health and drinking water. And there are various types of water. Ionic water generator is a system with special function, and can be classified as a medical device and should be manufactured after approval from the Food and Drug Administration. Basically ionized water is different from the packaged and stored water. When the tap water or ground water passes through the various filters of ionic water generator, it turns to the purified water of pH7 ~ 7.5 and we can electrolyze that water into anion and cation by diaphragm. And in negative electrode side, we can get alkaline water with calcium ($Ca^+$), potassium ($K^+$), magnesium ($Mg^+$), sodium ($Na^+$) for body. In general, we can change pH value from 5 to 9 of ionizer by controlling the level of electrolysis voltage in the ionizer. In general, 1stage (pH8), 2stage (pH8.5), 3stage (pH9), 4stage (pH9.5) are used as the alkaline ionized water, -1Stage (pH6.0), -2 stage (pH5.0) are used as the acidic water. But in early stage, the water that passed through filter was weakly alkaline water and that was problem. Therefore, when filter condition is stable, the pH and ORP value of water is different with the early one. the initial setting pH value of the ionizer was confirmed that changes significantly. In order to resolve this problem we need to wash filter for some period time and neutralize by acidification treatment of the filter.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.51 no.4
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• pp.351-361
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• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• Bulletin of the Korean Chemical Society
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• v.10 no.5
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• pp.414-418
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• 1989

The electrochemical behavior of cadmium(Ⅱ) in tartrate solution has been studied over the pH range of 6 to 13.6 in order to explain the phenomena of the changes in limiting current depending on the pH. The polarographic limiting current showed a constant value up to pH of 7.8, after which it decreased sharply to show a minimum at pH between 11 and 12. The limiting current, then, increased again with increasing pH. The number of peaks in cyclic voltammogram was 1 to 3 depending on the pH of the solution. Two other voltammetric peaks could be observed when the main reduction peak diminished. The decrease of limiting current at 7.5$Cd(C_4H_3O_6)^-$. The increase of limiting current at strong alkaline solution, however, was due to the complex $Cd(Tart)_2(OH)_2^{4-}$.

• Journal of Aquaculture
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• v.18 no.4
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• pp.245-251
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• 2005

This study was investigated the condition of their maximum activity to assay the enzymes of rotifer, Brachionus rotundiformis의 $\alpha$-amylase, total alkaline Protease, trypsin and TG-lipase activities of rotifer were higher and more sensitive in phosphate-NaOH buffer than Tris-HCl buffer. $\alpha$-amylase, trypsin and TG-lipase activities were appeared the maximum at pH 8.0, and total alkaline protease activity showed the maximum activity at pH 7.0. $\alpha$-amylase activity showed the highest activity at $40^{\circ}C$, and total alkaline protease and trypsin activities were assayed the highest at $55{\~}60^{\circ}C$. However, TG-lipase activity was appeared the highest at $25{\~}30^{\circ}C$. The optimum substrate concentration of enzyme activity of a-amylase, total alkaline protease, rypsin and TG-lipase were $3.5\%$ starch, $\0.6%$ azo-casein, $87.5{\mu}M$ BApNA and 81.2 mM olive oil, respectively. The optimum reaction time of enzyme activity of $\alpha$-amylase, total alkaline protease, trypsin and TG-lipase were increased up to 40, 60, 30 and 25 min., respectively. The data obtained in this study could be used for the digestive enzyme research of rotifer, B. rotundiformis.

• Parasites, Hosts and Diseases
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• v.31 no.4
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• pp.353-362
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• 1993

The present study was carried out to investigate the localization and isozyme patterns of acid phosphatase and alkaline phosphatase in metacercariae and in adults of F. seoulensis by enzyme-histochemistry method and electrophoresis. Acidphosphatase showed a strong activity at pH 5 in the intestinal caecum of adults, but showed no reactions in the nonsubstrate control and in the inhibitor-treated control. Alkaline phosphatase showed a strong activity at pH 8 in the intestinal caecum and the tribocytic organ of adults, and in the intestinal caecum and in the genital anlagen of metacercariae. In non-denature PAGE, ten bands of protein fraction from the extracts of metacercariae and twenty-two bands from adults were detected. In denature PAGE, two protein bands having molecular weights of 192 kDa and 123 kDa were detected in the metacercariae, but absent from adult stage. In adults, protein fractions of 27.5 kDa, 24.5 kDa, 21.4 kDa, 18 kDa, 16 kDa and 15 kDa were detected. In non-denature PAGE, isozymes of acid phosphatase showed the most strong activity at pH 5, whereas no activity was shown at pH 2 and pH 7. One isozyme 85 kDa, 73 kDa and 62 kDa) in adults.

• Korean Chemical Engineering Research
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• v.54 no.1
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• pp.101-107
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• 2016

This paper investigates the feasibility of applying the jet loop reactor for the neutralization of alkaline wastewater using carbon dioxide ($CO_2$). In this study, pH changes and $CO_2$ removal characteristics were examined by changing influent flow rate of alkaline wastewater (initial pH=10.1) and influent $CO_2$ flow rates. Influent flow rates of alkaline wastewater ($Q_{L,in}$) ranged between 0.9 and 6.6 L/min, and inlet gas flow rate ($Q_{G,in}$) of 1 and 6 L/min in a lab-scale continuous flow jet loop reactor. The outlet pH of wastewater was maintained at 7.2 when the ratio ($Q_{L,in}/Q_{G,in}$) of $Q_{L,in}$ and $Q_{G,in}$ was 1.1. However, the $CO_2$ removal efficiency and the outlet pH of wastewater were increased when $Q_{L,in}/Q_{G,in}$ ratio was higher than 1.1. Throughout the experiments, the maximum $CO_2$ removal efficiency and the outlet pH of wastewater were 98.06% and 8.43 at the condition when $Q_{G,in}$ and $Q_{L,in}$ were 2 L/min and 4 L/min, respectively.

• Proceedings of the KSME Conference
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• 2008.11b
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• pp.2415-2418
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• 2008

Polydiacetylenes (PDAs) are very attractive chemical substances which have distinctive features of color change and fluorescence emission by thermal or chemical stress. Especially, when PDAs contact with solutions of a particular pH, such as a strong alkaline sodium hydroxide (NaOH) solution or a strong acidic hydrogen chloride (HCl) solution, PDAs change their color from non-fluorescent blue to fluorescent red. In this study, we propose a novel method to detect alkaline pH using PDAs and NaOH solutions by hydrodynamic focusing on a microfluidic chip. Preliminary results indicate that the fluorescent intensity of PDAs increases in respond to the NaOH solution concentrations. Also, the fluorescence is quenched back when the PDAs are in contact with a HCl solution. These results are useful in a microfluidic PDA sensor chip design for pH detection.

• Journal of Applied Biological Chemistry
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• v.49 no.4
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• pp.135-139
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• 2006

A alkalophilic strain, Bacillus licheniformis MH31 producing an alkaline protease was isolated from mine soil of Boryeong in Korea. Production of a high level of alkaline protease was achieved 42 h after incubation when the bacterium was grown at pH 9.0 and $35^{\circ}C$ in Horikoshi medium supplemented with 0.5%(w/v) starch and 1%(w/v) skim milk as carbon and nitrogen source, respectively. The molecular weight of partially purified enzyme was estimated to be 30 kDa by SDS-PAGE and its optimum pH was pH 10. The enzyme showed optimum temperature at $50^{\circ}C$, and was stable up to $60^{\circ}C$ after 1 h incubation. The protease was strongly inhibited by 1 mM of PMSF which was known well as strong inhibitor of serine proteases, but almost not inhibited by 5 mM of EDTA and 1,10-phenanthroline. When the protein hydrolysis products of 1% skim milk by partially purified protease was compared with available commercial proteases using HPLC analysis, most of hydrolysis products were detected below molecular weight of 10,000 and the hydrolysis ratio of purified enzyme was 24.8% lower than those(above 32%) of commercial proteases.