Abstract：
:To address the bottlenecks of laccase-based catalysis, i.e., poor long-term stability and potential secondary pollution caused by synthetic mediator, we fabricated a new biocatalyst (N-PS-Lac) through adsorption of laccase onto polystyrene anion exchangers (N-PS) binding quaternary ammonium groups. After 2-year storage, the residual activity of N-PS-Lac remained as high as 101.7%, while that for native laccase was only 14.6%. Also, N-PS-Lac exhibited improved durability against pH variation and thermal treatment at 60°C. Gaussian curve fitting of FT-IR spectra indicated that laccase conformation of N-PS-Lac was rigidified, possibly because of the host geometric restriction and the host-laccase electrostatic attraction. A two-step method, i.e., adsorption of an azo dye AO7 by N-PS and then ectopic degradation by the immobilized laccase, was proposed to reuse the mediator HOBT for seven cyclic runs, where N-PS-Lac kept the constant decolorization efficiency. AO7 solution was detoxified completely after decolorization by the two-step method.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Zhang X,Pan B,Wu B,Zhang W,Lv Ldoi
10.1016/j.biortech.2014.04.105subject
Has Abstractpub_date
2014-07-01 00:00:00pages
248-53eissn
0960-8524issn
1873-2976pii
S0960-8524(14)00645-2journal_volume
164pub_type
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