Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/329380
Type: Artigo
Title: Biochemical And Biophysical Properties Of A Metagenome-derived Gh5 Endoglucanase Displaying An Unconventional Domain Architecture
Author: 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.; Neto
Mario de Oliveira; Squina
Fabio M.; Alvarez
Thabata M.
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.
Subject: Lignocellulosic Biomass
Glycoside Hydrolase Family 5
Calx-beta Domain
Editor: Elsevier Science BV
Amsterdam
Citation: International Journal Of Biological Macromolecules. Elsevier Science Bv, v. 99, p. 384 - 393, 2017.
Rights: fechado
Identifier DOI: 10.1016/j.ijbiomac.2017.02.075
Address: http://www-sciencedirect-com.ez88.periodicos.capes.gov.br/science/article/pii/S0141813016309291?via%3Dihub
Date Issue: 2017
Appears in Collections:Unicamp - Artigos e Outros Documentos

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