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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-beta-xylanase identified in a microbial consortium

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Autor(es):
Evangelista, Danilo Elton [1] ; Arnoldi Pellegrin, Vanessa de Oliveira [1] ; Santo, Melissa Espirito [1] ; McQueen-Mason, Simon [2] ; Bruce, Neil C. [2] ; Polikarpov, Igor [1]
Número total de Autores: 6
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ York, Dept Biol, Wentworth Way, York YO10 5DD, N Yorkshire - England
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Applied Microbiology and Biotechnology; v. 103, n. 19, p. 8035-8049, OCT 2019.
Citações Web of Science: 0
Resumo

Biotechnologies that aim to produce renewable fuels, chemicals, and bioproducts from residual ligno(hemi)cellulosic biomass mostly rely on enzymatic depolymerization of plant cell walls (PCW). This process requires an arsenal of diverse enzymes, including xylanases, which synergistically act on the hemicellulose, reducing the long and complex xylan chains to oligomers and simple sugars. Thus, xylanases play a crucial role in PCW depolymerization. Until recently, the largest xylanase family, glycoside hydrolase family 11 (GH11) has been exclusively represented by endo-catalytic beta-1,4- and beta-1,3-xylanases. Analysis of a metatranscriptome library from a microbial lignocellulose community resulted in the identification of an unusual exo-acting GH11 beta-1,4-xylanase (MetXyn11). Detailed characterization has been performed on recombinant MetXyn11 including determination of its low-resolution small-angle X-ray scattering (SAXS) molecular envelope in solution. Our results reveal that MetXyn11 is a monomeric globular enzyme that liberates xylobiose from heteroxylans as the only product. MetXyn11 has an optimal activity in a pH range from 6 to 9 and an optimal temperature of 50 degrees C. The enzyme maintained above 65% of its original activity in the pH range 5 to 6 after being incubated for 72 h at 50 degrees C. Addition of the enzyme to a commercial enzymatic cocktail (CelicCtec3) promoted a significant increase of enzymatic hydrolysis yields of hydrothermally pretreated sugarcane bagasse (16% after 24 h of hydrolysis). (AU)

Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
Beneficiário:Igor Polikarpov
Linha de fomento: Auxílio à Pesquisa - Temático
Processo FAPESP: 11/20505-4 - Duas classes importantes de glicosil hidrolases: estudos funcionais e análise estrutural
Beneficiário:Marco Antonio Seiki Kadowaki
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery
Beneficiário:Igor Polikarpov
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 11/21608-1 - Identificação e caracterização de novas enzimas com potencial na digestão de biomassa lignocelulósica
Beneficiário:Bruno Luan Soares Paula de Mello
Linha de fomento: Bolsas no Brasil - Doutorado Direto