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

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]

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

• 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
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• 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
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 11/20505-4 - Duas classes importantes de glicosil hidrolases: estudos funcionais e análise estrutural
• Beneficiário: Marco Antonio Seiki Kadowaki
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado