The Secretome of Phanerochaete chrysosporium and Trametes versicolor Grown in Microcrystalline Cellulose and Use of the Enzymes for Hydrolysis of Lignocellulosic Materials (2020)
- Authors:
- USP affiliated authors: SILVA, TATIANE DA FRANCA - EEL ; MILAGRES, ADRIANE MARIA FERREIRA - EEL ; SEGATO, FERNANDO - EEL ; FERRAZ, ANDRÉ LUIS - EEL ; MACHADO, ANGELA DA SILVA - EEL ; VALADARES, FERNANDA DE LIMA - EEL
- Unidade: EEL
- DOI: 10.3389/fbioe.2020.00826
- Assunto: CANA-DE-AÇÚCAR
- Keywords: basidiomycetes; biorefinery; cellobiohydrolases; glucoside hydrolases; secretome; white-rot fungi
- Agências de fomento:
- Language: Inglês
- Abstract: The ability of white-rot fungi to degrade polysaccharides in lignified plant cell walls makes them a suitable reservoir for CAZyme prospects. However, to date, CAZymes from these species are barely studied, which limits their use in the set of choices for biomass conversion in modern biorefineries. The current work joined secretome studies of two representative white-rot fungi, Phanerochaete chrysosporium and Trametes versicolor, with expression analysis of cellobiohydrolase (CBH) genes, and use of the secretomes to evaluate enzymatic conversion of simple and complex sugarcane-derived substrates. Avicel was used to induce secretion of high levels of CBHs in the extracellular medium. A total of 56 and 58 proteins were identified in cultures of P. chrysosporium and T. versicolor, respectively, with 78–86% of these proteins corresponding to plant cell wall degrading enzymes (cellulolytic, hemicellulolytic, pectinolytic, esterase, and auxiliary activity). CBHI predominated among the plant cell wall degrading enzymes, corresponding to 47 and 34% of the detected proteins in P. chrysosporium and T. versicolor, respectively, which confirms that Avicel is an efficient CBH inducer in white-rot fungi. The induction by Avicel of genes encoding CBHs (cel) was supported by high expression levels of cel7D and cel7C in P. chrysosporium and T. versicolor, respectively. Both white-rot fungi secretomes enabled hydrolysis experiments at 10 FPU/g substrate, despite the varied proportions of CBHs and other enzymes present in each case. When low recalcitrance sugarcane pith was used as a substrate, P. chrysosporium and T. versicolor secretomes performed similarly to Cellic® CTec2. However, the white-rot fungi secretomes were less efficient than Cellic® CTec2 during hydrolysis of more recalcitrant substrates, such as acid or alkaline sulfite-pretreated sugarcane bagasse, likely because Cellic® CTec2 contains an excess of CBHs compared with the white-rot fungi secretomes.General comparison of the white-rot fungi secretomes highlighted T. versicolor enzymes for providing high glucan conversions, even at lower proportion of CBHs, probably because the other enzymes present in this secretome and CBHs lacking carbohydrate-binding modules compensate for problems associated with unproductive binding to lignin.
- Imprenta:
- Source:
- Título: Frontiers in bioengineering and biotechnology
- ISSN: 22964185
- Volume/Número/Paginação/Ano: v., n. , p.1-15, 2020
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
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ABNT
MACHADO, ANGELA S. et al. The Secretome of Phanerochaete chrysosporium and Trametes versicolor Grown in Microcrystalline Cellulose and Use of the Enzymes for Hydrolysis of Lignocellulosic Materials. Frontiers in bioengineering and biotechnology, n. , p. 1-15, 2020Tradução . . Disponível em: https://doi.org/10.3389/fbioe.2020.00826. Acesso em: 14 fev. 2026. -
APA
MACHADO, A. N. G. E. L. A. S., Valadares, F. de L., Silva, T. da F., Milagres , A. M. F., Segato, F., & Ferraz, A. L. (2020). The Secretome of Phanerochaete chrysosporium and Trametes versicolor Grown in Microcrystalline Cellulose and Use of the Enzymes for Hydrolysis of Lignocellulosic Materials. Frontiers in bioengineering and biotechnology, ( ), 1-15. doi:10.3389/fbioe.2020.00826 -
NLM
MACHADO ANGELAS, Valadares F de L, Silva T da F, Milagres AMF, Segato F, Ferraz AL. The Secretome of Phanerochaete chrysosporium and Trametes versicolor Grown in Microcrystalline Cellulose and Use of the Enzymes for Hydrolysis of Lignocellulosic Materials [Internet]. Frontiers in bioengineering and biotechnology. 2020 ;( ): 1-15.[citado 2026 fev. 14 ] Available from: https://doi.org/10.3389/fbioe.2020.00826 -
Vancouver
MACHADO ANGELAS, Valadares F de L, Silva T da F, Milagres AMF, Segato F, Ferraz AL. The Secretome of Phanerochaete chrysosporium and Trametes versicolor Grown in Microcrystalline Cellulose and Use of the Enzymes for Hydrolysis of Lignocellulosic Materials [Internet]. Frontiers in bioengineering and biotechnology. 2020 ;( ): 1-15.[citado 2026 fev. 14 ] Available from: https://doi.org/10.3389/fbioe.2020.00826 - The secretome of two representative lignocellulose-decay basidiomycetes growing on sugarcane bagasse solid-state cultures
- In site produced and Commercially alkali-active xylanases compared for xylan exxtraction from sugarcane bagasse
- Comparative evaluation of acid and alkaline sulfite pretreatments for enzymatic saccharification of bagasses from three different sugarcane hybrids
- Fate of p-hydroxycinnamates and structural characteristics of residual hemicelluloses and lignin during alkaline-sulfite chemithermomechanical pretreatment of sugarcane bagasse
- Topochemical characterization of sugar cane pretreated with alkaline sulfite
- Topochemical characterization of sugar cane pretreated with alkaline sulfite
- Sugarcane hybrids with original low lignin contents and high field productivity are useful to reach high glucose yields from bagasse
- Anatomic and ultrastructural characteristics of different regions of sugar cane internodes which affect their response to alkaline-sulfite pretreatment and material recalcitrance
- Análise da expressão dos genes da via de biossíntese de hemicelulose em híbridos contrastantes de cana-de-açúcar (Saccharum app.))
- Uso de basidiomicetos no tratamento de bagaço de cana como etapa prévia aos processos de hidrólise enzimática dos polissacarídeos
Informações sobre o DOI: 10.3389/fbioe.2020.00826 (Fonte: oaDOI API)
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