Immobilization of Trametes versicolor laccase on LDH/alginate composite beads for improved textile dyes decolorization

Abstract

Laccase is an oxido-reductase known for its applications in biomass valorization (lignin depolymerization), in fine chemicals (building-blocks synthesis) or in environment (wastewater treatment). It works with molecular oxygen and produces water as its only by-product. However, its practical use remains limited due to the low stability and poor reusability of free laccase. To overcome these challenges, laccase from Trametes versicolor was immobilized onto layered double hydroxide and alginate composite beads by a glutaraldehyde cross-linker to create an easily separable and stable enzyme. Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), X-ray diffraction spectroscopy (XRD) and energy-dispersive X-ray spectroscopy (EDX) were used to characterize the as-synthesized composite beads (laccase@MgFe(LDH)/alginate). The activity of the immobilized laccase was measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) model substrate. Here, the optimal conditions of laccase immobilization were explored and the effects of various conditions of immobilization, pH, storage stability and thermal resistance of the (laccase@MgFe(LDH)/alginate) were also studied. The results revealed that the optimal conditions for laccase immobilization were a concentration of glutaraldehyde of 2.5 %, an amount of laccase (0.5 U/mg) of 2 mg/mL, and an immobilization time of 6 h. The stability of (laccase@MgFe(LDH)/alginate) was >70 % of its initial activity, even after 10 cycles. The study of dye decolorization showed up to 74 % of methylene blue (MB) and 69 % of Crystal violet (CV) degradation, suggesting the use of immobilized laccase on MgFe(LDH)/alginate composite beads as a promising and environmentally friendly tool for the degradation of environmental pollutants, in particular for the removal of textile dyes from wastewater.