Abstract

Species from the genus Talaromyces produce useful biomass-degrading enzymes and secondary metabolites. However, these enzymes and secondary metabolites are still poorly understood and have not been explored in depth because of a lack of comprehensive genetic information. Here, we report a 36.51-megabase genome assembly of Talaromyces pinophilus strain 1–95, with coverage of nine scaffolds of eight chromosomes with telomeric repeats at their ends and circular mitochondrial DNA. In total, 13,472 protein-coding genes were predicted. Of these, 803 were annotated to encode enzymes that act on carbohydrates, including 39 cellulose-degrading and 24 starch-degrading enzymes. In addition, 68 secondary metabolism gene clusters were identified, mainly including T1 polyketide synthase genes and nonribosomal peptide synthase genes. Comparative genomic analyses revealed that T. pinophilus 1–95 harbors more biomass-degrading enzymes and secondary metabolites than other related filamentous fungi. The prediction of the T. pinophilus 1–95 secretome indicated that approximately 50% of the biomass-degrading enzymes are secreted into the extracellular environment. These results expanded our genetic knowledge of the biomass-degrading enzyme system of T. pinophilus and its biosynthesis of secondary metabolites, facilitating the cultivation of T. pinophilus for high production of useful products.

Highlights

  • Talaromyces pinophilus, formerly designated Penicillium pinophilum, is a fungus that produces biomass-degrading enzymes such as α-amylase[1], cellulase[2], endoglucanase[3], xylanase[2], laccase[4] and α-galactosidase[2]

  • We found 489 genes from T. cellulolyticus Y-94 contained insertion-deletion mutations when mapping PE reads from the T. pinophilus [1–95] to the genome of T. cellulolyticus Y-94; 257 of these occurred in coding sequence regions

  • This study describes the nearly complete genome sequence of a member of the genus Talaromyces

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Summary

Introduction

Talaromyces pinophilus, formerly designated Penicillium pinophilum, is a fungus that produces biomass-degrading enzymes such as α-amylase[1], cellulase[2], endoglucanase[3], xylanase[2], laccase[4] and α-galactosidase[2]. The fungal strain T. pinophilus [1–95] was isolated from the soil of a dried, ploughed field in Wuzhou, China. This strain produces a highly efficient, calcium-independent α-amylase[1]. We describe the de novo whole-genome assembly of T. pinophilus strain [1–95], a nearly complete genome sequence of a high biomass-degrading enzyme-producing species in the genus Talaromyces. Comparative genomic analysis suggested that T. pinophilus harbors more biomass-degrading enzymes and secondary metabolites than other related filamentous fungi. The predicted secretory protein patterns of T. pinophilus [1–95] were analyzed

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