Effects of nonionic surfactant Triton X-100 on the laccase-catalyzed conversion of bisphenol A

Ji, Guanglei; Zhang, Haibo; Huang, Feng; Huang, Xirong

doi:10.1016/s1001-0742(08)62444-4

Cited by 50 publications

(27 citation statements)

References 30 publications

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“…Previous studies also investigated the effects of additives on the removal of phenol catalyzed by enzymes. Ji et al (2009) found that the addition of Trtion X-100 can improve the removal of bisphenol A with laccase. Tonegawa et al (2003) reported that biosurfactant rhamnolipid, as well as PEG, Tween 20 and Trtion X-100, can enhance the removal of 2,4-dichlorophenol with minced horseradish.…”

Section: Effect Of Surfactant Typementioning

confidence: 99%

“…Laccase (EC 1.10.3.2) is one of the best known multicopper enzymes and catalyzes the oxidation of a variety of aromatic compounds, in particular phenolic substrates, coupled to the reduction of molecular oxygen to water (Cañas et al 2007;Canfora et al 2008;Qiu and Huang 2010). However, some actions, such as the interactions of phenoxyl radicals with the active center of enzymes and the adsorption of enzymes onto the polymer products of phenol formed during the reaction, can lead to the enzyme inactivation during the oxidation of phenols (Ji et al 2009;Kulys and Ivanec-Goranina 2009;Modaressi et al 2005;Sakurai et al 2003). Several studies have shown that the addition of surfactants can prevent enzyme inhibitions (Ji et al 2009;Kulys and Ivanec-Goranina 2009;Liu et al 2008).…”

Section: Introductionmentioning

confidence: 99%

“…However, some actions, such as the interactions of phenoxyl radicals with the active center of enzymes and the adsorption of enzymes onto the polymer products of phenol formed during the reaction, can lead to the enzyme inactivation during the oxidation of phenols (Ji et al 2009;Kulys and Ivanec-Goranina 2009;Modaressi et al 2005;Sakurai et al 2003). Several studies have shown that the addition of surfactants can prevent enzyme inhibitions (Ji et al 2009;Kulys and Ivanec-Goranina 2009;Liu et al 2008). In addition, the interactions between enzyme and surfactant may induce a change in the conformation and/or active site of the enzyme, thereby increasing the enzyme's activity and stability (Karbassi et al 2003;Yang et al 2007).…”

Section: Introductionmentioning

confidence: 99%

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Effect of dirhamnolipid on the removal of phenol catalyzed by laccase in aqueous solution

Liu

Zeng

Zhong

et al. 2011

World J Microbiol Biotechnol

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In this study, the effects of three surfactants, i.e. the anionic biosurfactant dirhamnolipid (diRL), the cationic surfactant hexadecyltrimethyl ammonium bromide (CTAB), and the anionic surfactant sodium dodecyl sulfate (SDS), on the removal of phenol catalyzed by laccase were studied first. CTAB and SDS were detrimental, while diRL improved phenol removal and was selected for detailed research. The biosurfactant increased the activity of laccase and the removal of phenol with the increase of diRL concentrations from 10.6 to 318 μM. DiRL at 318 μM improved the removal when the initial concentrations of phenol were from 50 to 400 mg/l. In particular, the removal of phenol with 318 μM diRL was 4.3-6.4 folds that of the controls within 24 h when the initial concentration of phenol was 400 mg/l. The presence of diRL at 318 μM also caused the complete removal (above 98%) of phenol at concentrations from 50 to 400 mg/l after 24 h. The enhancement of phenol removal was over a wide range of pH and temperatures, and the highest removal efficiency was obtained at pH 6.0 and 50°C. The results suggest that diRL had potential application in the enhancement of phenols removal catalyzed by laccase in water treatment or remediation.

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Section: Effect Of Surfactant Typementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of dirhamnolipid on the removal of phenol catalyzed by laccase in aqueous solution

Liu

Zeng

Zhong

et al. 2011

World J Microbiol Biotechnol

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“…32 Several traditional disperser solvents were studied including methanol, ethanol, acetonitrile and acetone. The surfactant can also serve as the disperser solvent and accelerate the emulsification of carbon tetrachloride in water under the energy provided by ultrasound.…”

Section: Effect Of Disperser Solventmentioning

confidence: 99%

“…31 Triton X-100 has been widely applied in heavy-duty industrial cleaning and as agrochemical. 32 It is also an effective and economic emulsifier, wetting agent, phase dispersant 33 and solubilizer. 34 The aim of this work was to develop a method of UASEME for the determination of estrogens in water samples.…”

Section: Introductionmentioning

confidence: 99%

Ultrasound-assisted surfactant-enhanced emulsification microextraction combined with hplc for the determination of estrogens in water

Zou

Jin

et al. 2012

J. Braz. Chem. Soc.

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detector de arranjo de diodos para a determinação de 17β-estradiol (βE2), estrona (E1) e dietilestilbestrol (DES) em água. Ultrassom foi aplicado para auxiliar a emulsificação e Triton X-100 foi usado como dispersor e emulsificante. Tetracloreto de carbono foi usado como solvente extrator. Empregando otimização global, o procedimento foi caracterizado por um intervalo linear aceitável de 10 a 1000 ng mL -1 para βE2, E1 e DES (r > 0,997), exatidão e precisão validadas (RSD 0,85-1,28% (n = 5)) e alta sensibilidade com limites de detecção de 0,200, 0,100 e 0,125 ng mL -1 para βE2, E1 e DES, respectivamente. O procedimento foi aplicado para a análise de amostras típicas de água, com fatores de enriquecimento de 85,29, 173,45 e 97,05 para βE2, E1 e DES, respectivamente, e boas recuperações (≥ 89,82%). De maneira geral, o procedimento desenvolvido foi simples e confiável, com potencial de aplicação em larga escala para análises da água.An ultrasound-assisted surfactant-enhanced emulsification microextraction (UASEME) combined with high performance liquid chromatography-diode array detector procedure was developed for the determination of 17β-estradiol (βE2), estrone (E1) and diethylstilbestrol (DES) in water. Ultrasound was applied to assist emulsification, and Triton X-100 was adopted as the disperser and emulsifier. Carbon tetrachloride was applied as the extraction solvent. Global optimization was used and the developed procedure was characterized by an acceptable linear range of 10 to 1000 ng mL -1 for βE2, E1 and DES (r > 0.997), a validated accuracy and precision (RSD 0.85-1.28% (n = 5)), and high sensitivity with limits of detection of 0.200, 0.100 and 0.125 ng mL -1 for βE2, E1 and DES, respectively. Furthermore, we applied this procedure to analyze typical water samples, with enrichment factors of 85.29, 173.45 and 97.05 for βE2, E1 and DES, respectively, and good recoveries (≥ 89.82%). Altogether, the proposed procedure was simple and reliable, with potential application in large-scale water analysis.

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The biotechnological potential of subtilisin‐like fibrinolytic enzyme from a newly isolated Lactobacillus plantarum KSK‐II in blood destaining and antimicrobials

Kotb

2014

Biotechnology Progress

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An antimicrobial oxidative- and SDS-stable fibrinolytic alkaline protease designated as KSK-II was produced by Lactobacillus plantarum KSK-II isolated from kishk, a traditional Egyptian food. Maximum enzyme productivity was obtained in medium containing 1% lactose and 0.5% soybean flour as carbon and nitrogen sources, respectively. Purification of enzyme increased its specific activity to 1,140-fold with a recovery of 33% and molecular weight of 43.6 kDa. Enzyme activity was totally lost in the presence of ethylenediaminetetraacetic acid and was restored after addition of Fe(2+) suggesting that KSK-II is a metalloprotease and Fe(2+) acts as cofactor. Enzyme hydrolyzed not only the natural proteins but also synthetic substrates, particularly Suc-Ala-Ala-Pro-Phe-pNA. KSK-II can hydrolyze the Lys-X easier than Arg-X; thus, it was considered as a subtilisin-family protease. Its apparent Km , Vmax , and Kcat were 0.41 mM, 6.4 µmol mg(-1) min(-1) , and 28.0 s(-1) , respectively. KSK-II is industrially important from the perspectives of its maximal activity at 50°C (stable up to 70°C), ability to function at alkaline pH (10.0), stability at broad pH ranges (7.5-12.0) in addition to its stability toward SDS, H2 O2 , organic solvents, and detergents. We emphasize for the first time the potential of fibrinolytic activity for alkaline proteases used in detergents especially in blood destaining.

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Effects of nonionic surfactant Triton X-100 on the laccase-catalyzed conversion of bisphenol A

Cited by 50 publications

References 30 publications

Effect of dirhamnolipid on the removal of phenol catalyzed by laccase in aqueous solution

Effect of dirhamnolipid on the removal of phenol catalyzed by laccase in aqueous solution

Ultrasound-assisted surfactant-enhanced emulsification microextraction combined with hplc for the determination of estrogens in water

The biotechnological potential of subtilisin‐like fibrinolytic enzyme from a newly isolated Lactobacillus plantarum KSK‐II in blood destaining and antimicrobials

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