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Open AccessArticle

Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes

1
Key Laboratory of Eco-Textiles, Ministry of Education, Jiangnan University, Wuxi 214122, China
2
National Engineering Laboratory for Cereal Fermentation Technology & School of Biotechnology, Jiangnan University, Wuxi 214122, China
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2013, 14(6), 12520-12532; https://doi.org/10.3390/ijms140612520
Received: 11 February 2013 / Revised: 3 June 2013 / Accepted: 6 June 2013 / Published: 14 June 2013
(This article belongs to the Section Biochemistry)
The TiO2-montmorillonite (TiO2-MMT) complex was prepared by blending TiO2 sol and MMT with certain ratio, and its properties as an enzyme immobilization support were investigated. The pristine MMT and TiO2-MMT calcined at 800 °C (TiO2-MMT800) were used for comparison to better understand the immobilization mechanism. The structures of the pristine MMT, TiO2-MMT, and TiO2-MMT800 were examined by HR-TEM, XRD and BET. SEM was employed to study different morphologies before and after laccase immobilization. Activity and kinetic parameters of the immobilized laccase were also determined. It was found that the TiO2 nanoparticles were successfully introduced into the MMT layer structure, and this intercalation enlarged the “d value” of two adjacent MMT layers and increased the surface area, while the calcination process led to a complete collapse of the MMT layers. SEM results showed that the clays were well coated with adsorbed enzymes. The study of laccase activity revealed that the optimum pH and temperature were pH = 3 and 60 °C, respectively. In addition, the storage stability for the immobilized laccase was satisfactory. The kinetic properties indicated that laccase immobilized on TiO2-MMT complexes had a good affinity to the substrate. It has been proved that TiO2-MMT complex is a good candidate for enzyme immobilization. View Full-Text
Keywords: montmorillonite; laccase; enzyme immobilization; TiO2 montmorillonite; laccase; enzyme immobilization; TiO2
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MDPI and ACS Style

Wang, Q.; Peng, L.; Li, G.; Zhang, P.; Li, D.; Huang, F.; Wei, Q. Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes. Int. J. Mol. Sci. 2013, 14, 12520-12532. https://doi.org/10.3390/ijms140612520

AMA Style

Wang Q, Peng L, Li G, Zhang P, Li D, Huang F, Wei Q. Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes. International Journal of Molecular Sciences. 2013; 14(6):12520-12532. https://doi.org/10.3390/ijms140612520

Chicago/Turabian Style

Wang, Qingqing; Peng, Lin; Li, Guohui; Zhang, Ping; Li, Dawei; Huang, Fenglin; Wei, Qufu. 2013. "Activity of Laccase Immobilized on TiO2-Montmorillonite Complexes" Int. J. Mol. Sci. 14, no. 6: 12520-12532. https://doi.org/10.3390/ijms140612520

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