Potentialities of active membranes with immobilized laccase for Bisphenol A degradation

Int J Biol Macromol. 2018 Mar:108:837-844. doi: 10.1016/j.ijbiomac.2017.10.177. Epub 2017 Oct 31.

Abstract

Herein, we report the development of immobilized laccase based membrane bioreactor as a novel bio-catalytic system for the degradation of emerging endocrine disruptor i.e., Bisphenol A. Two laccase forms i.e. (1) in-house isolated and purified from an indigenous white-rot fungi Pycnoporus sanguineus (CS43) and (2) Trametes versicolor (commercial laccase from Sigma-Aldrich®) were immobilized on a multi-channel ceramic membrane (1.4μm in diameter) using 4% glutaraldehyde as a cross-linking agent. The immobilization yield and bisphenol A degradation activities of immobilized laccases were recorded at various pH levels. The surface topographies of immobilized-laccase membranes were accessed by scanning electron microscopy. In this study, 100% degradation of bisphenol A (20mg/L) was achieved in less than 24h in the presence of laccase from P. sanguineus (CS43) (620.55±14.85U/L) and T. versicolor (620.55±14.85U/L). The enzymes showed an optimal activity at pH 5 and 5.4 with a degradation rate of 204.8±1.8 and 79.0±0.1μmol/min/U for P. sanguineus (CS43) and T. versicolor, respectively. In conclusion, the highest immobilization of unit per square centimeter and efficient degradation potentiality strongly recommend the newly developed immobilized laccase based membrane bioreactor as a novel tool to tackle emerging contaminants degradation issues.

Keywords: Bisphenol A; Enzymatic degradation; Immobilization; Laccase; Membrane reactor.

MeSH terms

  • Benzhydryl Compounds / chemistry*
  • Bioreactors
  • Catalysis
  • Enzyme Activation
  • Enzymes, Immobilized*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Laccase / chemistry*
  • Laccase / metabolism
  • Molecular Structure
  • Phenols / chemistry*

Substances

  • Benzhydryl Compounds
  • Enzymes, Immobilized
  • Phenols
  • Laccase
  • bisphenol A