Coriolopsis trogii MUT3379: A Novel Cell Factory for High-Yield Laccase Production

Author:

Mellere Luca12ORCID,Bellasio Martina3,Berini Francesca1ORCID,Marinelli Flavia1ORCID,Armengaud Jean4ORCID,Beltrametti Fabrizio2ORCID

Affiliation:

1. Department of Biotechnology and Life Sciences, University of Insubria, 21100 Varese, VA, Italy

2. BioC-CheM Solutions S.r.l., Insubrias BioPark, 21040 Gerenzano, VA, Italy

3. Actygea S.r.l., Insubrias BioPark, 21040 Gerenzano, VA, Italy

4. Département Médicaments et Technologies pour la Santé (DMTS), CEA, INRAE, SPI, Université Paris-Saclay, 30200 Bagnols-sur-Cèze, France

Abstract

Coriolopsis trogii is a basidiomycete fungus which utilizes a large array of lignin-modifying enzymes to colonize and decompose dead wood. Its extracellular enzymatic arsenal includes laccases, i.e., polyphenol oxidases of relevant interest for different industrial applications thanks to their ability to oxidize a diverse range of natural and synthetic compounds. In this work, the production of laccases in C. trogii MUT3379 was explored and improved. From an initial production of ca. 10,000 U L−1, the fermentation process was gradually optimized, reaching a final yield of ca. 200,000 U L−1. An SDS-PAGE analysis of the secretome highlighted the presence of a main protein of ca. 60 kDa showing laccase activity, which was designated as Lac3379-1 once its primary sequence was established by tandem mass spectrometry. The characterization of Lac3379-1 revealed a remarkable enzymatic stability in the presence of surfactants and solvents and a diversified activity on a broad range of substrates, positioning it as an interesting tool for diverse biotechnological applications. The high-yield and robust production process indicates C. trogii MUT3379 as a promising cell factory for laccases, offering new perspectives for industrial applications of lignin-modifying enzymes.

Funder

University of Insubria

Publisher

MDPI AG

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