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The genus  Trichoderma  includes species of great biotechnological value, both for their mycoparasitic activities and for their ability to produce extracellular hydrolytic enzymes. Although activity of extracellular laccase has previously been reported in  Trichoderma  spp., the possible number of isoenzymes is still unknown, as are the structural and functional characteristics of both the genes and the putative proteins. In this study, the system of laccases  sensu stricto  in the  Trichoderma  species, the genomes of which are publicly available, were analyzed using bioinformatic tools. The intron/exon structure of the genes and the identification of specific motifs in the sequence of amino acids of the proteins generated  in silico  allow for clear differentiation between extracellular and intracellular enzymes. Phylogenetic analysis suggests that the common ancestor of the genus possessed a functional gene for each one of these enzymes, which is a characteristic preserved in  T. atroviride  and  T. virens . This analysis also reveals that  T. harzianum  and  T. reesei  only retained the intracellular activity, whereas  T. asperellum  added an extracellular isoenzyme acquired through horizontal gene transfer during the mycoparasitic process. The evolutionary analysis shows that in general, extracellular laccases are subjected to purifying selection, and intracellular laccases show neutral evolution. The data provided by the present study will enable the generation of experimental approximations to better understand the physiological role of laccases in the genus  Trichoderma  and to increase their biotechnological potential.

Structural and Phylogenetic Analysis of Laccases from Trichoderma: A Bioinformatic Approach