• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 1998.11a
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• pp.174-177
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• 1998

The effects of surfactants affecting polycyclic Aromatic Hydrocarbon(PAHs) solubility and biodegradation in soil slurry were investigated. The critical micelle concentration(CMC) values of surfactants used in this study were 12.7mg/L(Brij 30), 13.4mg/L(Tween 80), 13.6mg/t(Triton X-100). The solubility of PAH increased as the Hydrophile-Lipophile Balance(HLB) value of surfactant decrease. At surfactant biodegradation and toxicity experiement using respirometer, Brij 30 did not show any toxic effect and substrate inhibition upon the level of 1.5g/L. Also, biodegradation of Brij 30 gave no reduction on the phenanthrene biodegradation rate. When the desorption rate of phenanthrene between sand and clay is compared, lower percentage of phenanthrene was desorbed at clay because of the larger surface aera and higher organic content of clay. At the biodegradation experiments of phenanthrene in soil slurry phase, more than 90% of initial phenanthrene adsorbed onto both sand and clay were biodegraded by phenanthrene- acclimated cultures.

• Journal of Environmental Science International
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• v.12 no.1
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• pp.87-92
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• 2003

Synchronous spectrofluorimetry was carried out for the simultaneous determination of various polycyclic aromatic hydrocarbons(PAHs) in aqueous solution by fluorescence spectrometry have been studied. The optimal wavelength interval(${\triangle}{\lambda}$) for synchronous spectra of acenaphthene, anthracene, benzo[a]anthracene, fluorene and pyrene were investigated in the presence of surfactants. The great enhancement of the fluorescence of these PAHs in Triton X-100 was obtained and optimal wavelength was 50 nm. The calibration curves in synthetic mixture solution of 5 PAHs were linear over the range from $1.0{\times}10^{-8}M$ to $1.0{\tiems}10^{-4}M$. Under the optimal experimental conditions, the detection limits were $4.9{\tiems}10^{-9}M$,\;7.0{\times}10^{-9}M,\;4.7{\tiems}10^{-9}M,\;1.6{\tiems}10^{-9}M$ and $3.2{\tiems}10^{-9}M$ for acenaphthene, anthracene, benzo[a]anthracene, fluorene and pyrene, respectively.

• Fashion & Textile Research Journal
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• v.11 no.3
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• pp.465-468
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• 2009

In this study, acid cellulase was used to treat denim fabrics by varying pH, temperature, enzyme concentration, treatment time and non-ionic surfactant (Triton X-100) concentration. Treatment condition was controlled based on the weight loss. The characteristics of enzyme-treated fabrics were measured in terms of tearing strength, stiffness, and color difference. The optimum conditions for cellulase treatment of denim fabric were pH 5.0, $50^{\circ}C$, 3% (o.w.f.), 90minutes. The weight loss did not change significantly with the addition of a non-ionic surfactant, but it improved when more non-ionic surfactant were used. The tearing strength of enzyme-treated denim fabrics did not deteriorate. The stiffness of the treated fabrics improved with the enzymatic treatment with and without the non-ionic surfactant. The difference in color of fabrics treated with enzyme increased.

• Journal of the Korean Society of Clothing and Textiles
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• v.32 no.7
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• pp.1075-1081
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• 2008

Eco-friendly processing using enzymes has been focused in textile industry in order to reduce environmental pollutions. This paper was suggested to hydrolyze non-cellulose, such as fats and waxes in cotton fabrics by lipase treatment. Enzymatic treatment conditions were controlled according to pH, temperature, enzyme concentration, and treatment time. The physical properties of the lipase-treated cotton fabrics were evaluated by measuring weight loss, moisture regain and dyeing properties. The surface morphology of lipase-treated cotton fabrics were observed by SEM. As a result, the optimum conditions for the lipase treatment were at pH 4.2, temperature 50$^{\circ}C$, concentration 50%, and treatment time 90 minutes. Calcium chloride and Triton X-100 were effective auxiliaries in lipase treatment.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2006.04a
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• pp.153-156
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• 2006

유류오염토양의 자연복원 시 생물이용도(bioavailability)를 높이기 위해 사용되는 계면활성제의 영향을 살펴보고자 제지 폐수로부터 분리한 미생물과 5가지 계면활성제를 사용하였다. 계면활성제로는 Brij 35, Brij 30, Triton X-100, Tween 40, Tween 80을 사용하였으며 유류오염물질로는 PAHs를 사용하여 계면활성제 별 미생물의 성장률 및 PAHs 분해율을 살펴보았다. 그 결과 각각의 계면활성제에 따라 서로 다른 미생물 성장 및 PAHs 분해능을 보였다. 계면활성제에 따른 미생물 성장은 Tween 계열에서 뚜렷했으며 이들 중 Tween 40에서는 PAHs의 분해능 또한 가장 활발하였다.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2006.04a
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• pp.162-165
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• 2006

유해성 유기물질로 오염된 토양의 복원을 위한 토양세척공정에서 계면활성제를 선택적으로 재이용하기 위해 활성탄을 이용한 흡착 칼럼의 성능을 평가하였다. 계면활성제로는 Triton X-100을 소수성 유해 유기물질로는 다환방향족 탄화수소의 하나인 phenanthrene를 사용하여 그 성능을 평가하였다. 계면활성제의 흡착은 phenartthrene에 비해 빠른 흡착 특성을 보였으며 phenanthrene은 계면활성제의 포화흡착상태에서도 지속적으로 흡착이 이루어졌다. 이는 계면활성제의 흡착이 종료된 이후에도 유해성 유기물질의 지속적인 흡착을 기대할 수 있어 계면활성제의 지속적인 재이용과 활성탄 사용시간의 증대를 가져올 수 있음을 의미한다. 이와 같은 활성탄 칼럼에서의 유해성 유기물질의 우수한 선택적 흡착 결과는 기본적으로 소수성 정도의 차이와 size exclusion에 의한 기작뿐만 아니라 활성탄에 흡착된 계면활성제에 의한 다환방향족 탄화수소의 추가적인 흡착이 일어나 전체적인 성능이 향상되는 것에 기인한다.

• Proceedings of the Korean Society of Soil and Groundwater Environment Conference
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• 2005.04a
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• pp.178-181
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• 2005

토양세척 공정 시 오염물질을 제거하기 위해 사용한 계면활성제를 재사용하기 위해 활성탄을 사용하였으며 이때 계면활성제와 HOC (Hydrophobic Organic Chemical)의 분배를 예측 할 수 있는 모델을 개발하였다. 계면활성제로는 Triton X-100, HOC는 phenanthrene을 활성탄으로는 Darco 20-40 mesh를 사용하였다. 개발된 모델로 계면활성제 주입량, 활성탄 주입량에 따른 계면활성제와 HOC의 분배결과를 각각 전산 모사를 통하여 얻었다. 그 결과 활성탄이 포함된 계 내에서의 계면활성제와 HOC의 분배가 미셀이 형성되는 농도를 전후로 서로 다른 분배 양상을 보였다. 또한 전산모사 결과는 실제 실험결과를 비교적 정확하게 반영함을 알 수 있다.

• Bulletin of the Korean Chemical Society
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• v.23 no.7
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• pp.943-947
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• 2002

The two reactions between iron ion (Fe3+ ) and o-chlorophenylfluorone (o-CPF) and copper ion (Cu2+ ) and o-CPF are sensitive at pH 6 in the presence of Triton X-100. We have determined the formation constants of the complexes by the spectral correction technique. Because of the poor selectivity of o-CPF to metals, the competition coordination of only the iron ion from the Cu-o-CPF complex was found and applied to the selective detection of iron traces by the Selective Competition Coordination Determination (SCCD) approach.The analysis of several samples shows that the relative standard deviations are less than 5.0% and the recovery of iron ions between 94.5% and 106%.

• BMB Reports
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• v.28 no.6
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• pp.552-555
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• 1995

Treatment of microsomal vesicles isolated from etiolated Pisum sativum L cv. Alaska epicotyl tissue with agents inhibiting protein dephosphorylation, namely NaF and/or ATP, resulted in increased binding of the phytotropin NPA to the putative auxin efflux carriers localized on the plasma membrane. The phytotropin effect was especially conspicuous if the vesicles were simultaneously treated with Triton X-100. Kinetic analysis of the binding indicated the existance of two distinct sites for NPA, each having different affinities. Increased binding of the phytotropin to the membrane where protein dephosphorylation was inhibited was attributable to the increased ligand affinity of both sites. Treatment of tissue segments with flubride was found to enhance in vivo auxin transport. Implications of covalent modification of the auxin efflux carrier complex for the regulation of membrane transport of auxin molecules are discussed.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.52-59
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• 1988

A partially purified preparation of L-galactonolactone oxidase which catalyzes the last step of L-ascorbic acid biosynthesis was obtained from Saccharomyces cerevisiae ATCc 26787. The purification procedures included Triton X-100 treatment, protamine sulfate precipitation, ammonium sulfate precipitation, DEAE-Sepharose CL-6B ion exchange chromatography, Sephadex G-150 gel filtration chromatography, and Phenyl-Sepharose CL-4B hydrophobic interaction chromatography. The optimum temperature for the enzyme activity was about $34^{\circ}C$ and the optimum pH was 6.8-7.0. The substrate specificity was confined to L-aldonolactones, L-galactono-1,4-lactone and L-gulono-1,4-lactone. An apparent Km value of 0.294mM with L-galactono-1,4-lactone as a substrate was found. By comparing the substrate specificities of this enzyme with those of isofunctional enzymes of higher plants and animals, it becomes evident that the enzyme of S. cerevisiae ATCC 26787 is rather similar to the L-gulonolactone oxidase of animals than the galactonolactone dehydrogenase of higher plants.