Protein profile in Aspergillus nidulans recombinant strains overproducing heterologous enzymes

Author(s)

Zubieta, Mariane Paludetti ; Contesini, Fabiano Jares ; Rubio, Marcelo Ventura ; de Souza Schmidt Goncalves, Any Elisa ; Gerhardt, Jaqueline Aline ; Prade, Rolf Alexander ; de Lima Damasio, Andre Ricardo

• Document type: Journal article
• Source: MICROBIAL BIOTECHNOLOGY; v. 11, n. 2, p. 13-pg., 2018-03-01.

Abstract

Filamentous fungi are robust cell factories and have been used for the production of large quantities of industrially relevant enzymes. However, the production levels of heterologous proteins still need to be improved. Therefore, this article aimed to investigate the global proteome profiling of Aspergillus nidulans recombinant strains in order to understand the bottlenecks of heterologous enzymes production. About 250, 441 and 424 intracellular proteins were identified in the control strain Anid_pEXPYR and in the recombinant strains Anid_AbfA and Anid_Cbhl respectively. In this context, the most enriched processes in recombinant strains were energy pathway, amino acid metabolism, ribosome biogenesis, translation, endoplasmic reticulum and oxidative stress, and repression under secretion stress (RESS). The global protein profile of the recombinant strains Anid_AbfA and Anid_Cbhl was similar, although the latter strain secreted more recombinant enzyme than the former. These findings provide insights into the bottlenecks involved in the secretion of recombinant proteins in A.nidulans, as well as in regard to the rational manipulation of target genes for engineering fungal strains as microbial cell factories. (AU)

• FAPESP's process: 12/20549-4 - Secretion of heterologous glycoproteins in Aspergillus: effect of glycosylation pattern in functional parameters of glycosyl hydrolases
• Grantee: André Ricardo de Lima Damasio
• Support Opportunities: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants