Identification, characterization and functional expression of auxiliary activity e...
| Full text | |
| Author(s): |
Hahn Schneider, Willian Daniel
[1]
;
Goncalves, Thiago Augusto
[2, 3]
;
Uchima, Cristiane Akemi
[3]
;
Couger, Matthew Brian
[4]
;
Prade, Rolf
[4]
;
Squina, Fabio Marcio
[3]
;
Pinheiro Dillon, Aldo Jose
[1]
;
Camassola, Marli
[1]
Total Authors: 8
|
| Affiliation: | [1] Univ Caxias do Sul, Inst Biotechnol, Enzymes & Biomass Lab, Francisco Getulio Vargas St 1130, BR-95070560 Caxias Do Sul, RS - Brazil
[2] State Univ Campinas UNICAMP, Inst Biol, Dept Biochem, Sao Paulo - Brazil
[3] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Giuseppe Maximo Scolfaro 10-000, BR-13083970 Campinas, SP - Brazil
[4] Oklahoma State Univ, Dept Microbiol & Mol Genet, 1110 South Innovat Way, Stillwater, OK 74078 - USA
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | BIOTECHNOLOGY FOR BIOFUELS; v. 9, MAR 17 2016. |
| Web of Science Citations: | 23 |
| Abstract | |
Background: The enzymatic degradation of lignocellulosic materials by fungal enzyme systems has been extensively studied due to its effectiveness in the liberation of fermentable sugars for bioethanol production. Recently, variants of the fungus Penicillium echinulatum have been described as a great producer of cellulases and considered a promising strain for the bioethanol industry. Results: Penicillium echinulatum, wild-type 2HH and its mutant strain S1M29, were grown on four different carbon sources: cellulose, sugar cane bagasse pretreated by steam explosion (SCB), glucose, and glycerol for 120 h. Samples collected at 24, 96, and 120 h were used for enzymatic measurement, and the 96-h one was also used for secretome analysis by 1D-PAGE LC-MS/MS. A total of 165 proteins were identified, and more than one-third of these proteins belong to CAZy families. Glycosyl hydrolases (GH) are the most abundant group, being represented in larger quantities by GH3, 5, 17, 43, and 72. Cellobiohydrolases, endoglucanases, beta-glycosidases, xylanases, beta-xylosidases, and mannanases were found, and in minor quantities, pectinases, ligninases, and amylases were also found. Swollenin and esterases were also identified. Conclusions: Our study revealed differences in the two strains of P. echinulatum in several aspects in which the mutation improved the production of enzymes related to lignocellulosic biomass deconstruction. Considering the spectral counting analysis, the mutant strain S1M29 was more efficient in the production of enzymes involved in cellulose and hemicellulose degradation, despite having a nearly identical CAZy enzymatic repertoire. Moreover, S1M29 secretes more quantities of protein on SCB than on cellulose, relevant information when considering the production of cellulases using raw materials at low cost. Glucose, and especially glycerol, were used mainly for the production of amylases and ligninases. (AU) | |
| FAPESP's process: | 14/06923-6 - Sugar cane biomass recalcitrance: basic knowledge related to the cell wall construction, pretreatment and enzymatic digestion, applied for the development of innovative biorefinery models |
| Grantee: | Andre Luis Ferraz |
| Support type: | Program for Research on Bioenergy (BIOEN) - Thematic Grants |
| FAPESP's process: | 08/58037-9 - Library generation for biomass-conversion enzymes from soil metagenome |
| Grantee: | Fábio Márcio Squina |
| Support type: | Program for Research on Bioenergy (BIOEN) - Young Investigators Grants |
| FAPESP's process: | 12/19040-0 - Characterization of gene expression of Neurospora crassa in response to deconstruction of sugar cane bagasse |
| Grantee: | Cristiane Akemi Uchima |
| Support type: | Scholarships in Brazil - Post-Doctorate |