• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.441-445
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• 1987

The gene coding for alkaline amylase of alkalophilic Bacillus sp. AL-8 was cloned and expressed in Escherichia coli which was lack of amylase activity. For the cloning of the alkaline amylase gene, the chromosomal DNA and plasmid vector pBR322 were cleaved at the site of EcoRI and the gene was cloned. The selection of the transformants carrying the amylase gene was based on the their antibiotics resistance and amylase activity of the transformants. The recombinant plasmids pJW8 and pJW200 containing 5.8Kb and 3.0Kb EcoRI inserts respectively were proved to can the alkaline amylase gene. Alkaline amylase expressed in E. coli was characterized. The enzyme was proved to be stable at the range of alkaline pH.

• Journal of Soil and Groundwater Environment
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• v.20 no.6
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• pp.103-110
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• 2015

Nitro-aromatic Compounds (NACs) of explosives are structurally non-degradable materials that have an adverse effect to humans and ecosystems in case of emissions in natural due to the strong toxicity. In this study, batch test in the laboratory-scale has been conducted to find some process parameters of alkaline hydrolysis by considering the characteristics of NACs which are unstable in a base status and field application evaluation have been performed on the batch test results. Based on the experimental results of both laboratory and pilot-scale test, the optimum conditions of parameters for the alkaline hydrolysis of soils contaminated with explosives were pH 12.5, above the solid-liquid ratio 1 : 3, above the room temperature and 30 minute reaction time. In these four process parameters, the most important influencing factor was pH, and the condition of above pH 12.0 was necessary for high contaminated soils (more than 60 mg/kg). In the case of above pH 12.5, the efficiency of alkaline hydrolysis was very high regardless of the concentrations of contaminated soils. At pH 11.5, the removal efficiency of TNT was increased from 76.5% to 97.5% when the temperature in reactor was elevated from room temperature to 80℃. This result shows that it is possible to operate the alkaline hydrolysis at even pH 11.5 due to increased reaction rate depending on temperature adjustment. The results found in above experiments will be able to be used in alkaline hydrolysis for process improvement considering the economy.

• Textile Coloration and Finishing
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• v.8 no.1
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• pp.34-42
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• 1996

This Study was made to investigate alkaline dyeing systems for a new dyeing applicable polyester fibers. Disperse dyes for dyeing of polyester fibers were C.I. Red 60, Blue 56 and Yellow 54 as three primary colors of E type which used widely on the scene. Dyeing properties of dispers dyes on the polyester fibers are discussed according to variation of pH values for application of alkaline dyeing method compared with to ordinary acidic dyebath. Alkaline pH of the dyebath was controlled to pH 9 and 10.5 with buffer solutions using each hydrochloride and disodiumtetraborate, disodiumtetraborate and sodium hydroxide to promote the reproducibility of dyeing. Dyeing properties of dispers dyes on the polyester fibers by alkaline dyeing method compared with to ordinary acidic dyebath were discussed by estimation of color, wash-fastness, bleeding and migration of dyed polyester fabric.

• Nuclear Engineering and Technology
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• v.32 no.6
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• pp.595-604
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• 2000

Flow-Accelerated Corrosion Behavior of SA106 Gr.C steel in room temperature alkaline solution simulating the CANDU primary water condition was studied using Rotating Cylinder Electrode. Systems of RCE were set up and electrochemical parameters were applied at various rotating speeds. Corrosion current density decreased up to pH 10.4 then it increased rapidly at higher pH. This is due to the increasing tendency of cathodic and anodic exchange half-cell current. Corrosion potential shifted slightly upward with rotating velocity. Passive film was formed from pH 9.8 by the mechanism of step oxidation and the subsequent precipitation of ferrous species into hydroxyl compound. Above pH 10.4, the film formation process was active and the film became stable. Corrosion current density showed increment in pH 6.98 with the rotating velocity, while it soon saturated from 1000 rpm above pH 9.8. This seems that activation process which represents formation of passive film on the bare metal surface controls the entire corrosion process

• Journal of Food Hygiene and Safety
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• v.16 no.1
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• pp.33-36
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• 2001

V. parahaemolyticus possessed an extracellular alkaline protease activity during the stationary growth phase. Various factors such as initial pH of medium, incubation temperature and shaking rate were investigated far optimizing the production of alkaline protease from V. parahaemolyticus ATCC 17802. Maximal activity of the protease was obtained when the bacteria were grown in 2% skim milk medium in 0.1M tris/HCl buffer (pH 7.6). Maximal activity of the protease was obtained when the bacteria were growls at initial pH of 7.6, incubation temperature 37$^{\circ}C$ and shaking rate of 250 rpm.

• Applied Biological Chemistry
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• v.37 no.5
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• pp.320-325
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• 1994

These studies were conducted to investigate the chemical composition changes in in vitro digestibility for the improvement of nutritive value of rice straw by alkaline hydrogen peroxide. The content of neutral detergent fiber (NDF), acid detergent fiber (ADF), hemicellulose, cellulose and lignin in rice straw was decreased with higher level of $H_2O_2\;(pH 11.5)$. The content of ADF, cellulose and ash of the rice straw washed after $H_2O_2\;(pH 11.5)$ treatment tended to be increased but NDF, hemicellulose and lignin were decreased with higher concentration of $H_2O_2\;(pH 11.5)$. In the rice straw washed after alkaline hydrogen peroxide treatment the decomposition of cellulose and lignin was effective in $pH\;11.5{\sim}12.5$, in smaller cutting size and $55^{\circ}C$. The in vitro organic matter digestibility was increased with higher $H_2O_2$ concentration and smaller cutting size of rice straw.

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.160-164
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• 1989

A 5.7Kb EcoRI fragment containing alkaline amylase gene of Bacillus sp. AL-8 obtained in the previons experiment (10) was transformed in B. subtilis via plasmid pUB110. The enzymatic proper-ties of the amylase produced by the transformants were Identical to those of the donor strain. Thus, the alkaline amylase activity from the transformant was maximum at pH 10 and 5$0^{\circ}C$. And the enzyme was very stable over the ranges of alkaline pH. In order to determine the location of the alkaline amylase gene within the 5.7Kb DNA fragment, the fragment was subcloned in E. coli. It was found that the alkaline amylase gene was located k EcoRI fragment of 3.7Kb.

• Applied Biological Chemistry
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• v.31 no.4
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• pp.356-360
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• 1988

The alkaline protease producing bacteria isolated from soil and identified as Bacillus subtilis. The optimum medium for alkaline protease production from the microorganism was as follows; soluble starch, 1.5% ; proteose peptone, 0.5% ; $K_2HPO_4$, 0.1% ; $MgSO_4{\cdot}7H_2O$, 0.02% and sodium carbonate, 1.0%. The optimum temperature for alkaline protease production was $35^{\circ}C$, and the initial pH of medium was pH 10.5. The alkaline protease activity was about 2,300 U per ml of culture broth by Casein-Folin Method. A 9.2 fold purification of alkaline protease was obtained from culture broth. The recovery was 14% and purified enzyme was identified as single band, and its molecular weight was about 19,000. The optimum temperature for enzyme reaction was $70^{\circ}C$, and optimum pH was 12. The activity of purified enzyme was inhibited by metal ion ($Fe^{++}$), and Phenylmethylsulfonyl Fluoride, a serine protease inhibitor.

• Food Science of Animal Resources
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• v.34 no.3
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• pp.307-315
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• 2014

pH adjustment would be of advantage in improving the water holding capacity of muscle proteins. The objective of this study was to evaluate the addition of fish sarcoplasmic protein (SP) solution, which was adjusted to pH 3.0 or 12.0, neutralized to pH 7.0, and lyophilized to obtain the acid- and alkaline-treated SP samples, on the functional properties of the chicken myofibrillar protein induced by microbial transglutaminase (MTG). The solubility of alkaline-treated SP was higher than that of the acid counterpart; however, those values of the two pH-treated samples were lower than that of normal SP (p<0.05). All SP solutions were mixed with myofibrillar proteins (MP) extracted from chicken breast, and incubated with MTG. The shear stresses of MP with acid- and alkaline-treated SP were higher than that of normal SP. The thermal stability of MP mixture reduced upon adding SP, regardless of the pH treatment. The breaking force of MP gels with acid-treated SP increased more than those of alkaline-treated SP, while normal SP showed the highest value. The MP gel lightness increased, but cooking loss reduced, with the addition of SP. Smooth microstructure of the gel surface was observed. These results indicated that adjusting the pH of SP improved the water holding capacity of chicken myofibrillar proteins induced by MTG.

• Applied Biological Chemistry
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• v.43 no.3
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• pp.169-173
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• 2000

For the development of enzyme detergent capable of effectively washing at low temperature, a bacterium producing alkaline protease was isolated from soil samples, and properties of the enzyme were investigated. The selected strain was Gram negative, rod shape$(0.6{\sim}0.7{\times}1.3{\sim}2.6\;{\mu}m\;in\;size)$ and motile. It had the degradation activity of aesculin, gelatin and casein, and was catalase-positive. The cell wall components was meso-DAP, and G+C mole contents was 43.3%. From these results, the strain was identified as Acinetobacter sp. KN-27. The activity of alkaline protease by this strain peaked with 3,300 D.U/mL after 36 hours in the liquid culture at $40^{\circ}C$. The optimal pH and temperature of the enzyme were pH 9 and $60^{\circ}C$, respectively. Alkaline protease produced by Acinetobacter sp. KN-27 has shown two active bands on the electrophoresis of native gel.