Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion.
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.
Zhou
Gui-Ping
GP
Key Laboratory of Colloid & Interface Chemistry of the Education Ministry of China, Shandong University, Jinan 250100, People's Republic of China.
Zhang
Yun
Y
Huang
Xi-Rong
XR
Shi
Chuan-Hong
CH
Liu
Wei-Feng
WF
Li
Yue-Zhong
YZ
Qu
Yin-Bo
YB
Gao
Pei-Ji
PJ
D002384:Catalysis; D004655:Emulsions; D057927:Hydrophobic and Hydrophilic Interactions; D007093:Imidazoles / Q000737:chemistry*; D042845:Laccase / Q000378:metabolism*; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology; D014783:Viscosity
C412621:1-butyl-3-methylimidazolium hexafluorophosphate; D004655:Emulsions; D007093:Imidazoles; D042845:Laccase; D010544:Peroxidases; C042858:lignin peroxidase