Abstract

Contaminants deriving from human activities represent a constantly growing threat to our environment and have a direct impact on plant and animal health. To alleviate this ecological imbalance, biocatalysis offers a green and sustainable alternative to conventional chemical processes. Due to their broad specificity, laccases are enzymes possessing excellent potential for synthetic biotransformations in various fields as well as for the degradation of organic contaminants. Herein, we produced laccases in submerged cultures of P. ostreatus and T. versicolor in three different media. The fungi/medium combination leading to the highest enzymatic activity was malt extract (2%) + yeast extract (3%) + glucose (0.8%). Laccase production was further increased by supplementing this medium with different concentrations of Cu2+, which also provided a better understanding of the induction effect. Additionally, we disclose preliminary results on the interaction of laccases with mediators (ABTS and violuric acid - VA) for two main applications: lignin depolymerisation with guaiacylglycerol-β-guaiacyl ether (GBG) as lignin model and micropollutant degradation with Remazol Brilliant Blue (RBB) as enzymatic bioremediation model. Promising results were achieved using VA to increase depolymerization of GBG dimer and to enhance RBB decolorisation.

Highlights

  • Laccases (EC 1.10.3.2) are blue multicopper isozymes that are able to oxidise a wide range of phenols or arylamines

  • P. ostreatus grew in malt extract and in malt extract + yeast extract + glucose

  • Laccase produced by P. ostreatus reaches a maximum of 0.119 U/mL on day 13 in malt extract (Fig. 2A, blue triangles)

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Summary

Introduction

Laccases (EC 1.10.3.2) are blue multicopper isozymes that are able to oxidise a wide range of phenols or arylamines. The active site of laccases is composed of four copper atoms subclassified into different types of clusters (T1, T2 and T3) depending on their structural features.[3,4,5,6,7,8] These enzymes display a low specificity and nearly hundred different compounds have been identified as laccase substrates. In nature, they are capable of degrading structures as complex and recalcitrant as lignin.

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