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Secretomic insight into the biomass hydrolysis potential of the phytopathogenic fungus Chrysoporthe cubensis.
Tavares, Murillo Peterlini; Morgan, Túlio; Gomes, Riziane Ferreira; Rodrigues, Marina Quádrio Raposo Branco; Castro-Borges, William; de Rezende, Sebastião Tavares; de Oliveira Mendes, Tiago Antônio; Guimarães, Valéria Monteze.
Afiliación
  • Tavares MP; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • Morgan T; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • Gomes RF; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • Rodrigues MQRB; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • Castro-Borges W; Department of Biological Science, Universidade Federal de Ouro Preto, Campus Universitário Morro do Cruzeiro, Ouro Preto, MG 35400-000, Brazil.
  • de Rezende ST; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • de Oliveira Mendes TA; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil.
  • Guimarães VM; Department of Biochemistry and Molecular Biology, Universidade Federal de Viçosa, Av. PH Rolfs, s/n, Viçosa, MG 36570-900, Brazil. Electronic address: vmonteze@ufv.br.
J Proteomics ; 236: 104121, 2021 03 30.
Article en En | MEDLINE | ID: mdl-33540065
The phytopathogenic fungus Chrysoporthe cubensis has a great capacity to produce highly efficient enzymes for the hydrolysis of lignocellulosic biomass. The bioinfosecretome of C. cubensis was identified by computational predictions of secreted proteins combined with protein analysis using 1D-LC-MS/MS. The in silico secretome predicted 562 putative genes capable of encoding secreted proteins, including 273 CAZymes. Proteomics analysis confirmed the existence of 313 proteins, including 137 CAZymes classified as Glycosyl Hydrolases (GH), Polysaccharide Lyases (PL), Carbohydrate Esterases (CE) and Auxiliary Activities enzymes (AA), which indicates the presence of classical and oxidative cellulolytic mechanisms. The enzymes diversity in the extract shows fungal versatility to act in complex biomasses. This study provides an insight into the lignocellulose-degradation mechanisms by C. cubensis and allows the identification of the enzymes that are potentially useful in improving industrial process of bioconversion of lignocellulose. SIGNIFICANCE: Chrysoporthe cubensis is an important deadly canker pathogen of commercially cultivated Eucalyptus species. The effective depolymerisation of the recalcitrant plant cell wall performed by this fungus is closely related to its high potential of lignocellulolytic enzymes secretion. Since the degradation of biomass occurs in nature almost exclusively by enzyme secretion systems, it is reasonable to suggest that the identification of C. cubensis lignocellulolytic enzymes is relevant in contributing to new sustainable alternatives for industrial solutions. As far as we know, this work is the first accurate proteomic evaluation of the enzymes secreted by this species of fungus. The integration of the gel-based proteomic approach, the bioinformatic prediction of the secretome and the analyses of enzymatic activity are powerful tools in the evaluation of biotechnological potential of C. cubensis in producing carbohydrate-active enzymes. In addition, analysis of the C. cubensis secretome grown in wheat bran draws attention to this plant pathogen and its extracellular enzymatic machinery, especially regarding the identification of promising new enzymes for industrial applications. The results from this work allowed for explanation and reinforce previous research that revealed C. cubensis as a strong candidate to produce enzymes to hydrolyse sugarcane bagasse and similar substrates.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ascomicetos / Proteómica Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Brasil

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ascomicetos / Proteómica Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Brasil
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