Thermostability, pH stability and dye degrading activity of a bacterial laccase are enhanced in the presence of Cu2O nanoparticles

► The activity of laccase is enhanced at high temperature in presence of Cu2O-NP. ► NP-laccase retained its activity for 2h at 80°C. ► NP-laccase was found to be pH stable within the range of 4–12. ► NP-laccase had enhanced entropy enthalpy compensation at high temperatures. ► NP-laccase can be pote...

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Veröffentlicht in:Bioresource technology 2013-01, Vol.127, p.25-36
Hauptverfasser: Mukhopadhyay, Arka, Dasgupta, Anjan Kumar, Chakrabarti, Krishanu
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Sprache:eng
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Zusammenfassung:► The activity of laccase is enhanced at high temperature in presence of Cu2O-NP. ► NP-laccase retained its activity for 2h at 80°C. ► NP-laccase was found to be pH stable within the range of 4–12. ► NP-laccase had enhanced entropy enthalpy compensation at high temperatures. ► NP-laccase can be potentially used for phenolic and azo dye-decolorization. The present study relates to a nanotechnology enabled method in which purified laccase from Escherichia coli AKL2 was supplemented with 100μM copper oxide nanoparticles (Cu2O) (NP-laccase). The activity, half life and stability of NP-laccase were enhanced by 4, 42 and 36-fold respectively at high temperature (80°C) and also over a wide range of pH (4–12) than laccase (in the presence of 0.18mM CuSO4). Thermodynamic analysis of the nanoparticle-induced enzyme stability revealed an enhanced entropy–enthalpy compensation at 80°C, which reflected the maintenance of its native structure. This was further supported by CD studies. The enhanced activity and thermostability of NP-laccase can be utilized for efficient decolorisation of dyes (both phenolic and azo).
ISSN:0960-8524
1873-2976
DOI:10.1016/j.biortech.2012.09.087