Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion.
Identifieur interne : 000681 ( Main/Curation ); précédent : 000680; suivant : 000682Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion.
Auteurs : Gui-Ping Zhou [République populaire de Chine] ; Yun Zhang ; Xi-Rong Huang ; Chuan-Hong Shi ; Wei-Feng Liu ; Yue-Zhong Li ; Yin-Bo Qu ; Pei-Ji GaoSource :
- Colloids and surfaces. B, Biointerfaces [ 0927-7765 ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Imidazoles.
- enzymologie : Phanerochaete.
- isolement et purification : Peroxidases.
- métabolisme : Laccase, Peroxidases.
- Catalyse, Interactions hydrophobes et hydrophiles, Viscosité, Émulsions.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Imidazoles.
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Laccase, Peroxidases.
- chemical : Emulsions.
- enzymology : Phanerochaete.
- Catalysis, Hydrophobic and Hydrophilic Interactions, Viscosity.
Abstract
For hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]), an H(2)O-in-[BMIM][PF(6)] microemulsion could be formed in the presence of nonionic surfactant Triton X-100 (TX-100). In such a medium, both lignin peroxidase (LiP) and laccase could express their catalytic activity with the optimum molar ratio of H(2)O to TX-100 at 8.0 for LiP and >20 for laccase, and the optimum pH values at 3.2 for LiP and 4.2 for laccase, respectively. As compared with pure or water saturated [BMIM][PF(6)], in which the two oxidases had negligible catalytic activity due to the strong inactivating effect of [BMIM][PF(6)] on both enzymes, the use of the [BMIM][PF(6)]-based microemulsion had some advantages. Not only the catalytic activities of both fungal oxidases greatly enhanced, but also the apparent viscosity of the medium decreased.
DOI: 10.1016/j.colsurfb.2008.05.016
PubMed: 18602799
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pubmed:18602799Le document en format XML
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<term>Imidazoles (chemistry)</term>
<term>Laccase (metabolism)</term>
<term>Peroxidases (isolation & purification)</term>
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<front><div type="abstract" xml:lang="en">For hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF(6)]), an H(2)O-in-[BMIM][PF(6)] microemulsion could be formed in the presence of nonionic surfactant Triton X-100 (TX-100). In such a medium, both lignin peroxidase (LiP) and laccase could express their catalytic activity with the optimum molar ratio of H(2)O to TX-100 at 8.0 for LiP and >20 for laccase, and the optimum pH values at 3.2 for LiP and 4.2 for laccase, respectively. As compared with pure or water saturated [BMIM][PF(6)], in which the two oxidases had negligible catalytic activity due to the strong inactivating effect of [BMIM][PF(6)] on both enzymes, the use of the [BMIM][PF(6)]-based microemulsion had some advantages. Not only the catalytic activities of both fungal oxidases greatly enhanced, but also the apparent viscosity of the medium decreased.</div>
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