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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.)

Development and Biotechnological Application of a Novel Endoxylanase Family GH10 Identified from Sugarcane Soil Metagenome

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Alvarez, Thabata M. [1, 2] ; Goldbeck, Rosana [1] ; dos Santos, Camila Ramos [3] ; Paixao, Douglas A. A. [1] ; Goncalves, Thiago A. [1, 2] ; Franco Cairo, Joao Paulo L. [1, 2] ; Almeida, Rodrigo Ferreira [1] ; Pereira, Isabela de Oliveira [1] ; Jackson, George [1] ; Cota, Junio [1] ; Buechli, Fernanda [1, 2] ; Citadini, Ana Paula [1] ; Ruller, Roberto [1] ; Polo, Carla Cristina [3] ; Neto, Mario de Oliveira [4] ; Murakami, Mario T. [3] ; Squina, Fabio M. [1]
Total Authors: 17
[1] CNPEM, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP - Brazil
[2] Univ Estadual Campinas UNICAMP, Dept Bioquim, IB, Campinas, SP - Brazil
[3] CNPEM, Lab Nacl Biociencias LNBio, Campinas, SP - Brazil
[4] Univ Estadual Paulista UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: PLoS One; v. 8, n. 7 JUL 29 2013.
Web of Science Citations: 12

Metagenomics has been widely employed for discovery of new enzymes and pathways to conversion of lignocellulosic biomass to fuels and chemicals. In this context, the present study reports the isolation, recombinant expression, biochemical and structural characterization of a novel endoxylanase family GH10 (SCXyl) identified from sugarcane soil metagenome. The recombinant SCXyl was highly active against xylan from beechwood and showed optimal enzyme activity at pH 6,0 and 45 degrees C. The crystal structure was solved at 2.75 angstrom resolution, revealing the classical (beta/alpha)(8)-barrel fold with a conserved activesite pocket and an inherent flexibility of the Trp281-Arg291 loop that can adopt distinct conformational states depending on substrate binding. The capillary electrophoresis analysis of degradation products evidenced that the enzyme displays unusual capacity to degrade small xylooligosaccharides, such as xylotriose, which is consistent to the hydrophobic contacts at the +1 subsite and low-binding energies of subsites that are distant from the site of hydrolysis. The main reaction products from xylan polymers and phosphoric acid-pretreated sugarcane bagasse (PASB) were xylooligosaccharides, but, after a longer incubation time, xylobiose and xylose were also formed. Moreover, the use of SCXyl as pre-treatment step of PASB, prior to the addition of commercial cellulolytic cocktail, significantly enhanced the saccharification process. All these characteristics demonstrate the advantageous application of this enzyme in several biotechnological processes in food and feed industry and also in the enzymatic pretreatment of biomass for feedstock and ethanol production. (AU)

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: 10/11469-1 - Library generation for biomass-conversion enzymes from soil metagenome
Grantee:Thabata Maria Alvarez
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 11/20977-3 - Investigation of plant biomass conversion in termite Coptotermes gestroi complementary to glycosyl hydrolases aiming at bioproducts formation derived from lignocellulosic biomass.
Grantee:João Paulo Lourenço Franco Cairo
Support type: Scholarships in Brazil - Doctorate