Novel genetic tools that enable highly pure protein production in Trichoderma reesei

Sci Rep. 2019 Mar 22;9(1):5032. doi: 10.1038/s41598-019-41573-8.

Abstract

Trichoderma reesei is an established protein production host with high natural capacity to secrete enzymes. The lack of efficient genome engineering approaches and absence of robust constitutive gene expression systems limits exploitation of this organism in some protein production applications. Here we report engineering of T. reesei for high-level production of highly enriched lipase B of Candida antarctica (calB) using glucose as a carbon source. Multiplexed CRISPR/Cas9 in combination with the use of our recently established synthetic expression system (SES) enabled accelerated construction of strains, which produced high amounts of highly pure calB. Using SES, calB production levels in cellulase-inducing medium were comparable to the levels obtained by using the commonly employed inducible cbh1 promoter, where a wide spectrum of native enzymes were co-produced. Due to highly constitutive expression provided by the SES, it was possible to carry out the production in cellulase-repressing glucose medium leading to around 4 grams per liter of fully functional calB and simultaneous elimination of unwanted background enzymes.

MeSH terms

  • Cellulase / metabolism
  • Cellulose 1,4-beta-Cellobiosidase / genetics
  • Culture Media / pharmacology
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Gene Expression Regulation, Enzymologic / drug effects
  • Gene Expression Regulation, Enzymologic / genetics*
  • Gene Expression Regulation, Fungal / drug effects
  • Gene Expression Regulation, Fungal / genetics*
  • Genetic Engineering / methods*
  • Glucose / metabolism
  • Glucose / pharmacology
  • Industrial Microbiology / methods
  • Lipase / genetics*
  • Lipase / metabolism
  • Promoter Regions, Genetic / genetics
  • Reproducibility of Results
  • Trichoderma / genetics*
  • Trichoderma / metabolism

Substances

  • Culture Media
  • Fungal Proteins
  • Lipase
  • lipase B, Candida antarctica
  • Cellulase
  • Cellulose 1,4-beta-Cellobiosidase
  • Glucose