An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase-like multicopper oxidase on poly-3-hydroxybutyrate

Microb Biotechnol. 2018 Sep;11(5):881-892. doi: 10.1111/1751-7915.13287. Epub 2018 Jun 12.

Abstract

The presence of synthetic dyes in wastewaters generated by the textile industry constitutes a serious environmental and health problem that urges the scientific community on an appropriate action. As a proof-of-concept, we have developed a novel approach to design enzymatic bioreactors with the ability to decolorize dye solutions through the immobilization of the bacterial CueO laccase-like multicopper oxidase from Escherichia coli on polyhydroxybutyrate (PHB) beads by making use of the BioF affinity tag. The decolorization efficiency of the system was characterized by a series of parameters, namely maximum enzyme adsorption capacity, pH profile, kinetic constants, substrate range, temperature and bioreactor recycling. Depending on the tested dye, immobilization increased the catalytic activity of CueO by up to 40-fold with respect to the soluble enzyme, reaching decolorization efficiencies of 45-90%. Our results indicate that oxidase bioreactors based on polyhydroxyalkanoates are a promising alternative for the treatment of coloured industrial wastewaters.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bioreactors
  • Coloring Agents / metabolism*
  • Enzymes, Immobilized / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Hydrogen-Ion Concentration
  • Hydroxybutyrates / metabolism*
  • Kinetics
  • Oxidoreductases / metabolism*
  • Polyesters / metabolism*
  • Protein Binding
  • Substrate Specificity
  • Temperature
  • Wastewater / chemistry*
  • Water Pollutants, Chemical / metabolism*

Substances

  • Coloring Agents
  • Enzymes, Immobilized
  • Escherichia coli Proteins
  • Hydroxybutyrates
  • Polyesters
  • Waste Water
  • Water Pollutants, Chemical
  • poly-beta-hydroxybutyrate
  • Oxidoreductases
  • cueO protein, E coli