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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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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Author(s):
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]
Total Authors: 6
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: Applied Microbiology and Biotechnology; v. 103, n. 19, p. 8035-8049, OCT 2019.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 10/52362-5 - Targeted analysis of microbial lignocellulolytic secretomes: a new approach to enzyme discovery
Grantee:Igor Polikarpov
Support type: Regular Research Grants
FAPESP's process: 11/21608-1 - Identification and characterization of new enzymes with potential for lignocellulosic biomass conversion
Grantee:Bruno Luan Soares Paula de Mello
Support type: Scholarships in Brazil - Doctorate (Direct)