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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 and biophysical properties of a metagenome-derived GH5 endoglucanase displaying an unconventional domain architecture

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Pimentel, Agnes C. ; Ematsu, Gabriela C. G. ; Liberato, Marcelo V. ; Paixao, Douglas A. A. ; Franco Cairo, Joao Paulo L. ; Mandelli, Fernanda ; Tramontina, Robson ; Gandin, Cesar A. ; de Oliveira Neto, Mario ; Squina, Fabio M. ; Alvarez, Thabata M.
Total Authors: 11
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 99, p. 384-393, JUN 2017.
Web of Science Citations: 4
Abstract

Endoglucanases are key enzymes in the degradation of cellulose, the most abundant polymer on Earth. The aim of this work was to perform the biochemical and biophysical characterization of CelE2, a soil metagenome derived endoglucanase. CelE2 harbors a conserved domain from glycoside hydrolase family 5 (GH5) and a C-terminal domain with identity to Calx-beta domains. The recombinant CelE2 displayed preference for hydrolysis of oat beta-glucan, followed by lichenan and carboxymethyl cellulose. Optimum values of enzymatic activity were observed at 45 degrees C and pH 5.3, and CelE2 exhibited considerable thermal stability at 40 degrees C for up to 360 min. Regarding the cleavage pattern on polysaccharides, the release of oligosaccharides with a wide degree of polymerization indicated a characteristic of endoglucanase activity. Furthermore, the analysis of products generated from the cleavage of cellooligosaccharides suggested that CelE2 exhibited transglycosylation activity. Interestingly, the presence of CaCl2 positively affect CelE2, including in the presence of surfactants. SAXS experiments provided key information on the effect of CaCl2 on the stability of CelE2 and dummy atom and rigid-body models were generated. To the best of our knowledge this is the first biochemical and biophysical characterization of an endoglucanase from family GH5 displaying this unconventional modular organization. (C) 2017 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 14/12861-3 - Biochemical characterization of a metagenomic cellulase from family 5 and determination of biotechnological application
Grantee:Agnes Cristina Pimentel
Support type: Scholarships in Brazil - Scientific Initiation
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: 14/04105-4 - Structural and functional characterization of new cellulases, focusing in the relation between catalytic domains and CBMs
Grantee:Marcelo Vizoná Liberato
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 14/06923-6 - Sugar cane biomass recalcitrance: basic knowledge related to the cell wall construction, pretreatment and enzymatic digestion, applied for the development of innovative biorefinery models
Grantee:Andre Luis Ferraz
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants
FAPESP's process: 16/01926-2 - Influence of an accessory domain in biochemical and structural characteristics of the cellulase CelE2
Grantee:Agnes Cristina Pimentel
Support type: Scholarships in Brazil - Master
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