Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 122, Issue -, Pages 359-366Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.10.147
Keywords
Laccase; Entrapped-cross-linked enzyme aggregates; Porous silica; Immobilization; Phenol
Funding
- Tehran University of Medical Sciences (TUMS) Iran
- Iran National Science Foundation (INSF), Iran
- University of Tehran (UT), Iran
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Laccase was immobilized using a combinatorial strategy of cross-linking and entrapping in mesoporous silica to prepare entrapped enzyme species including simply adsorbed, entrapped cross-linked enzyme (E-CLE) and entrapped cross-linked enzyme aggregate (E-CLEA) to explore their potential in phenol removal. Parameters including pH, temperature, time and cross-linker concentration were optimized to achieve an immobilized product with highest laccase specific activity. Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM) and atomic force microscopy (AFM) were used to characterize the immobilization products. The storage and operational stability analysis were also carried out. Accordingly, E-CLEAs showed improved thermal and pH stabilities and activity retention in hydrophobic and hydrophilic solvents. Moreover, based on the resulted half-lives (t(1/2)) for free and insoluble laccases, the improved storage stability is reported for E-CLEAs at 1.71 and 20.88 days for them, respectively. In addition, the immobilized biocatalyst exhibited good operational stability and reusability through maintaining up to 79% of its initial activity after 20 cycles of successive operations. In conclusion, E-CLEAs have catalytic potential in efficient phenol removal and advantages of the insolubilized form of laccase as E-CLEAs make it an appealing system in applications such as possible treatment of phenol contaminated wastewater. (C) 2018 Elsevier B.V. All rights reserved.
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