An insight into cellulolytic capacity of the Trichoderma harzianum P49P11 revealed by omics approaches

Cellulases are a group of enzymes with several applications in biofuel production, and the paper, food, pharmaceutical, and chemical industries. Trichoderma harzianum P49P11 secrete all cellulases with high efficiency, representing an alternative to the current filamentous fungi in biotechnological industries. In this study, the cellulolytic mechanisms employed by the strain P49P11 to degrade crystalline cellulose in batch fermentation culture mode were elucidated by combining genome and secretome analysis. The strain P49P11 encodes nineteen cellulase genes from five different CAZyme families (GH5, GH6, GH7, GH12, and GH45), followed by several enzyme families for hemicellulose, pectin, and alpha-and beta-glucans degradation. The diverse CAZymes were also observed in the secretome, including cellulases, hemicellulases, and glucanases. In addition, β-glucosidases and xylanase activities detected during the fermentation process validated our secretome analysis. Taken together, our results revealed all enzymatic machinery used by the T. harzianum P49P11 to degrade cellulose in batch fermentation mode. Highlights We described a high-quality genome assembly and annotation of the T. harzianum P49P11. The T. harzianum P49P11 genome possesses a complete set of genes for lignocellulose degradation. The first report on T. harzianum P49P11 secretome obtained from batch fermentation strategy. T. harzianum P49P11 produced cellulases, lignocellulases, and auxiliary enzymes produced in response to crystalline cellulose.