dc.creatorSchneider
dc.creatorWDH; Goncalves
dc.creatorTA; Uchima
dc.creatorCA; Couger
dc.creatorMB; Prade
dc.creatorR; Squina
dc.creatorFM; Dillon
dc.creatorAJP; Camassola
dc.creatorM
dc.date2016
dc.date2016-12-06T18:32:04Z
dc.date2016-12-06T18:32:04Z
dc.date.accessioned2018-03-29T02:04:38Z
dc.date.available2018-03-29T02:04:38Z
dc.identifier
dc.identifierBiotechnology For Biofuels. BIOMED CENTRAL LTD, n. 9, n. 66, p. .
dc.identifier1754-6834
dc.identifierWOS:000372490700001
dc.identifier10.1186/s13068-016-0476-3
dc.identifierhttp://biotechnologyforbiofuels.biomedcentral.com.ez88.periodicos.capes.gov.br/articles/10.1186/s13068-016-0476-3
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/320439
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1311205
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionThe 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.
dc.description9
dc.description
dc.description
dc.description
dc.descriptionFAPESP (The State of Sao Paulo Research Foundation) [2008/58037-9, 2014/06923-6, 2012/19040-0]
dc.descriptionNational Council for Scientific and Technological Development (CNPq) [310186/2014-5, 442333/2014-5, 140796/2013-4]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description
dc.description
dc.description
dc.languageEnglish
dc.publisherBIOMED CENTRAL LTD
dc.publisherLONDON
dc.relationBiotechnology for Biofuels
dc.rightsfechado
dc.sourceWOS
dc.subjectLignocellulosic Biomass
dc.subjectBiofuels
dc.subjectPenicillium Echinulatum Strains
dc.subjectSecretome
dc.subjectCazymes
dc.titlePenicillium Echinulatum Secretome Analysis Reveals The Fungi Potential For Degradation Of Lignocellulosic Biomass
dc.typeArtículos de revistas


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