Immobilization of laccase on magnetic bimodal mesoporous carbon and the application in the removal of phenolic compounds

Liu, Yuanyuan; Zeng, Zhuotong; Zeng, Guangming; Tang, Lin; Pang, Ya; Li, Zhen; Liu, Can; Lei, Xiaoxia; Wu, Mengshi; Ren, Pinyun; Liu, Zhifeng; Chen, Ming; Xie, Guizhong

doi:10.1016/j.biortech.2011.11.015

Cited by 252 publications

(121 citation statements)

References 34 publications

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“…This peak-shift phenomenon can be explained by the electrostatic interaction influenced by the carrier microenvironment [26]. Similar behavior was also observed in other studies [26,27]. As seen in Figure 5a, the immobilized laccase generally showed a broader pH-activity profile than that of the free laccase, indicating that the immobilization methods preserved the enzyme activity in a wider pH range [28].…”

Section: The Coordination Of Metal Ions and Their Properties In Enzymsupporting

confidence: 86%

Laccase Immobilization by Chelated Metal Ion Coordination Chemistry

Wang

Cui

et al. 2014

Polymers

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Abstract:In this work, amidoxime polyacrylonitrile (AOPAN) nanofibrous membrane was prepared by a reaction between PAN nanofibers and hydroxylamine hydrochloride. The AOPAN nanofibrous membranes were used for four metal ions (Fe ) and also the four mixed metal ions were further used for laccase (Lac) immobilization. Compared with free laccase, the immobilized laccase showed better resistance to pH and temperature changes as well as improved storage stability. Among the four individual metal ion chelated membranes, the stability of the immobilized enzymes generally followed the order as Fe-AOPAN-Lac > Cu-AOPAN-Lac > Ni-AOPAN-Lac > Cd-AOPAN-Lac. In addition, the immobilized enzyme on the carrier of AOPAN chelated with four mixed metal ions showed the best properties.

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Section: The Coordination Of Metal Ions and Their Properties In Enzymsupporting

confidence: 86%

Laccase Immobilization by Chelated Metal Ion Coordination Chemistry

Wang

Cui

et al. 2014

Polymers

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“…The effect of temperature on laccase activity was studied in the range 20-50 ∘ C with a laccase concentration of 2.0 mM in 50 mM phosphate buffer pH 5. Results for pH and temperature are presented in a normalised form with the highest value of each set being assigned the value of 100% activity [22,23].…”

Section: Laccase Optimizationmentioning

confidence: 99%

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Mazlan

Hanifah

2017

International Journal of Polymer Science

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Immobilization of laccase on the functionalized methacrylate-acrylate copolymer microspheres was studied. Poly(glycidyl methacrylate-co-n-butyl acrylate) microspheres consisting of epoxy groups were synthesized using facile emulsion photocuring technique. The epoxy groups in poly(GMA-co-nBA) microspheres were then converted to amino groups. Laccase immobilization is based on covalent binding via amino groups on the enzyme surface and aldehyde group on the microspheres. The FTIR spectra showed peak at 1646 cm −1 assigned to the conformation of the polymerization that referred to GMA and nBA monomers, respectively. After modification of the polymer, intensity of FTIR peaks assigned to the epoxy ring at 844 cm −1 and 904 cm −1 was decreased. The results obtained from FTIR exhibit a good agreement with the epoxy content method. The activity of laccaseimmobilized microspheres increased upon increasing the epoxy content. Furthermore, poly(GMA-co-nBA) microspheres revealed uniform size below 2 m that contributes to large surface area of the microspheres to be used as a matrix, thus increasing the enzyme capacity and enzymatic reaction. Immobilized enzyme also shifted to higher pH and temperature compared to free enzyme.

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“…Bayramoglu et al [26] reported 81% residual activity of laccase immobilized on CHX-g-p(IA)-Cu(II) membrane, after 10th cycle of syringaldazine oxidation. Liu et al [34] reported 50% residual activity of laccase immobilized on CMMC support after 10th cycle of ABTS oxidation.…”

Section: Reusability Of Laccase Nanoparticlementioning

confidence: 99%

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

Gahlout

Rudakiya

Gupte³

2017

Int Nano Lett

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Immobilization of enzyme with nanostructures enhances its ideal characteristics, which may allow the enzyme to become more stable and resistant. The present investigation deals with the formulation of laccase nanosilica conjugates to overcome the problems associated with its stability and reusability. Synthesized nanosilica and laccase nanoparticles were spherical shaped, with the mean size of 220 and 615 nm, respectively. Laccase nanoparticles had an optimum temperature of 55°C and pH 4.0 for the oxidation of ABTS. Laccase nanoparticle retained 79% of residual activity till 20th cycle. It also showed 91% of its initial activity at lower temperatures even after 60 days. Laccase nanoparticles were applied for Reactive Violet 1 degradation wherein 96.76% of decolourization was obtained at pH 5.0 and 30°C within 12 h. Toxicity studies on microbes and plants suggested that the degraded metabolites were less toxic than control dye. Thus, the method applied for immobilization increased storage stability and reusability of laccase, and therefore, it can be utilized for efficient degradation of azo dyes.

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Immobilization of laccase on magnetic bimodal mesoporous carbon and the application in the removal of phenolic compounds

Cited by 252 publications

References 34 publications

Laccase Immobilization by Chelated Metal Ion Coordination Chemistry

Laccase Immobilization by Chelated Metal Ion Coordination Chemistry

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Laccase-conjugated amino-functionalized nanosilica for efficient degradation of Reactive Violet 1 dye

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