| Literature DB >> 24862000 |
Xiaolin Zhang1, Bingcai Pan2, Bing Wu1, Weiming Zhang1, Lu Lv1.
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.Entities:
Keywords: Degradation; Laccase; Long-term stability; Phytotoxicity; Polystyrene composite
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Year: 2014 PMID: 24862000 DOI: 10.1016/j.biortech.2014.04.105
Source DB: PubMed Journal: Bioresour Technol ISSN: 0960-8524 Impact factor: 9.642