• Journal of the Korean Applied Science and Technology
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• v.34 no.1
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• pp.33-40
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• 2017

To isolate and identify the yeast strains associated with D. morbifera, homogenized D. morbifera root samples were spread onto GPY, DG18, SCG and DOB agar media containing antibiotics, Triton X-100, and l-sorbose. Total 81 yeast isolates were analyzed by sequencing of internal transcribed spacer (ITS) region of the ribosomal DNA. The results showed that the root-associated yeast species were composed of the genera Vanderwaltozyma (40 isolates), Cryptococcus (40 isolates), and Kluyveromyces (one isolate). Moreover, the Kluyveromyces isolate exhibited high bioethanol productivity. In addition, the Vanderwaltozyma and Cryptococcus were dominant in D. morbifera roots. The specific yeast community associated with D. morbifera roots was identified by phylogenetic sequence analyses. These yeast isolates may have industrial applications as biosurfactant and bioethanol.

• Bulletin of the Korean Chemical Society
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• v.27 no.10
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• pp.1604-1608
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• 2006

A simple and efficient cloud point extraction-spectrofluorimetric method for the determination of thiamine in human urine is proposed. The procedure is based on the oxidation of thiamine with ferricyanide to form thiochrome, its extraction to Triton X-114 micelles and spectrofluorimetric determination. The variables affecting oxidation of thiamine, extraction and phase separation were studied and optimized. Under the experimental conditions used, the calibration graphs were linear over the range 2.5-1000 ng $mL^{-1}$. The limit of detection was 0.78 ng $mL^{-1}$ of thiamine and the relative standard deviation for 5 replicate determinations of thiamine at 400 ng $mL^{-1}$ concentration level was 2.42%. Average recoveries between 93-107% were obtained for spiked samples. The proposed method was applied to the determination of thiamine in human urine.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.1009-1011
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• 2004

In the present work a very simple, sensitive and selective spectrophotometric method for the determination of nitrite in micellar media is described. The method is based on the color reaction of nitrite with p-nitroaniline in the presence of diphenylamine in acid media. In order to remove the extraction step, Triton X-100, a non-ionic surfactant was used as micellar media. The optimum reaction conditions such as acid concentration, reagents concentration and effect of time have been studied and the analytical characteristics of the method such as limit of detection, linear range and molar absorptivity have been obtained. The interference of some anions and cations was also tested. The method was applied to the determination of nitrite in real samples.

• Journal of Environmental Science International
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• v.12 no.7
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• pp.783-789
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• 2003

This study was conducted to reuse the rice straw ash as washing agent for oil contaminated soils. The results are summarized as follows. The physical characteristics of rice straw before and after burning were as follows ; In case of burning rice straw 1g, the rice straw ash was generated 0.14g and pH was changed neutrality into alkali(pH 10.9) and specific surface area was increased to five times and particle distribution was corresponded to fine silt.(under 0.05mm) The physical characteristics of rice straw ash were Carbon 10.9%, Hydrogen 1.5%, Oxygen 23.4%, Nitrogen 5.2%, Sulfate 1.2% and chemical characteristics were Si 189.2ppm, Ca 10.2ppm, Mg 4.7ppm. Oil cleanup ratio by pH variation were about 40∼50% of initial concentration of oil by pH 10∼11. As the result of cleanup comparative experiment, the rice straw ash was about 20∼30%, the tritonX-100 about 40∼50% of washing efficiency, and then in the future it will be possibility of substitute washing agent.

• KSBB Journal
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• v.10 no.1
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• pp.30-37
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• 1995

Membrane-bound alcohol dehydrogenase(ADH) was purified to homogeneity from the acetic acid producing bacteria, Acetobacter sp. KM. The enzyme was solubilized and extracted with Triton X-100 and purified using the Mono-Q ion exchange chromatography and Superose 12 gel filtration chromatography. The enzyme was purified to 12-fold with a yield of 30%. The molecular weight of the purified enzyme was to be 335 KDa. SDS-PAGE of the enzyme showed two subunits with molecular weights of 79 KDa and 49 KDa. It indicated that the enzyme consisted of three subunits of the 79 KDa and two subunits of the 49 KDa. The purified .ADH preferentially oxidized straight chain aliphatic alcohol except methanol. Formaldehyde, acetaldehyde and glutaraldehyde were also oxidized. The apparent Km for ethanol was 1.04 mM and the optimum pH and temperature were 5.0∼6.0 and 32$^{\circ}C$, respectively. V2O5 and divalent cation such as ZnCl2 and NiCl2 inhibited enzymatic activity.

• KSBB Journal
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• v.15 no.3
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• pp.318-322
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• 2000

An oxygen-sensitive fumarate reductase has been purified from the cytosol fraction of the Enterococcus faecalis RKY1 grown anaerobically on a defined medium containing glycerol and fumarate. A major portion of the purification was performed with employing Triton X-100 and reducing agents by Phenyl-sepharose CL-4B DEAE-sepharose and Dephadex G-150 The final activity was 0.42 unit/mg. The deduced molecular mass of active band was 66 kDa. The optimal pH and temperature for the activity were 7.0 and 38$^{\circ}C$ respectively. The enzyme activity was not affected by 1mM metal ions such as bacl2 $.$2H2O HgCl2 MnCl2$.$4H2O ZnCl2 CuCl2$.$2H2O Mgcl2$.$6H2O FeSo4$.$7H2O and by EDTA. Partially purified enzyme ws yellow in color ; spectroscopic study indicated the presence of flavins as a cofactor.

• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.253-258
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• 1996

Stabilities of sweets potato f-amylase on various reagents were studied. The enzyme was stabilized by bovine serum albumin, Triton X-100 and 2-mercaptoethanol of 0.04%. Among them, bovine serum albumin was the most effective. And enzyme stability was increased by using the deairated solution. The enzyme activity was remained 0% in the absence of glycerol, 25% in the presence of 20% glycerol and 50% in the presence of 40% glycerol at 37$^{\circ}C$, for 15 hours in pH 11. SDS inhibited the enzyme, and 2-mercaptoethanol and dithiothreitol stabilized it.

• Biomedical Science Letters
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• v.18 no.2
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• pp.96-103
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• 2012

Kv 4.2 ion channel protein has an ability to open at subthreshold membrane potentials and to recover quickly from inactivation. That is very important for neuronal signal transmission in vertebrate brain. In order to purify Kv 4.2 protein, the novel purification methods were experimented. The purification procedure utilized chromatography on DE-52 ion exchange column and affinity chromatography on a WGA-Sepharose 4B, and Kv 4.2 affinity column chromatography. It was found that 0.5% (wt./vol.) Triton X-100 detergent in lysis buffer worked well for Kv 4.2 protein solubilization from rat brain membrane. Protein quantitative determination was conducted by BCA method at 562 nm for each purification step to avoid determination interference of protein at 280 nm by detergent. The confirmation of Kv 4.2 existence and amount is performed using by SDS-PAGE/immunoblotting or 96-well dot blotting. The Kv 4.2 without interacting protein that contains carbohydrate, was purified from novel biochemical 3-steps purification method for further research.

• Mycobiology
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• v.43 no.2
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• pp.157-162
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• 2015

Lichen-forming fungal proteins have been seldom searched due to many difficulties in their extraction. Phenols, quinones, proteases, and other components released during cell disruption have been known to be the greatest challenges related to protein extraction from lichens. To overcome these problems and maintain good electrophoretic resolution and high protein concentration, an extraction buffer containing polyvinylpolypyrrolidone, ascorbic acid, Triton X-100, polyethylene glycol, proteinase, and oxidase inhibitors in sodium phosphate buffer was developed. This extraction buffer showed high efficiency for all lichen species tested in the study.

• Journal of Environmental Science International
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• v.6 no.5
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• pp.481-488
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• 1997

Microorganisms capable of degrading trlchloroethylene(TCEI using phenol as a induction substrate were isolated from industrial effluents and soil. The strain MS-64K which had the highest blodegradablllty was identified as the genus Micrococcus. The optimal conditions of medium for the growth and blodegadatlon of trlchloroethylene were observed as follows; the initial pH 7.0, trlchloroethylene 1, 000ppm as the carbon source, 0.2% ${(NH_4)}_2SO_4$, as the nitrogen source. respectively. Lag period and degradation time on optimal medium were shorter than those on Isolation medium. Growth on the optimal medium was Increased. Addition of 0.1% Triton X-100 Increased the growth rate of Micrococcus sp. MS-64K, but degradation was equal to optimal medium. Trlchloroethylene degradation by Micrococcus sp. MS-64K was shown to fit logarithmic model when the compound was added at initial concentration of 1, 000ppm.