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

Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome

Full text
Author(s):
Show less -
Alvarez, Thabata M. [1] ; Paiva, Joice H. [2] ; Ruiz, Diego M. [2] ; Cairo, Joao Paulo L. F. [1] ; Pereira, Isabela O. [1] ; Paixao, Douglas A. A. [1] ; de Almeida, Rodrigo F. [1] ; Tonoli, Celisa C. C. [2] ; Ruller, Roberto [1] ; Santos, Camila R. [2] ; Squina, Fabio M. [1] ; Murakami, Mario T. [2]
Total Authors: 12
Affiliation:
[1] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Ciencia & Tecnol Bioetanol CTBE, Campinas, SP - Brazil
[2] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias LNBio, Campinas, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: PLoS One; v. 8, n. 12 DEC 17 2013.
Web of Science Citations: 21
Abstract

Cellulases play a key role in enzymatic routes for degradation of plant cell-wall polysaccharides into simple and economically-relevant sugars. However, their low performance on complex substrates and reduced stability under industrial conditions remain the main obstacle for the large-scale production of cellulose-derived products and biofuels. Thus, in this study a novel cellulase with unusual catalytic properties from sugarcane soil metagenome (CelE1) was isolated and characterized. The polypeptide deduced from the celE1 gene encodes a unique glycoside hydrolase domain belonging to GH5 family. The recombinant enzyme was active on both carboxymethyl cellulose and beta-glucan with an endo-acting mode according to capillary electrophoretic analysis of cleavage products. CelE1 showed optimum hydrolytic activity at pH 7.0 and 50 degrees C with remarkable activity at alkaline conditions that is attractive for industrial applications in which conventional acidic cellulases are not suitable. Moreover, its three-dimensional structure was determined at 1.8 angstrom resolution that allowed the identification of an insertion of eight residues in the beta 8-alpha 8 loop of the catalytic domain of CelE1, which is not conserved in its psychrophilic orthologs. This 8-residue-long segment is a prominent and distinguishing feature of thermotolerant cellulases 5 suggesting that it might be involved with thermal stability. Based on its unconventional characteristics, CelE1 could be potentially employed in biotechnological processes that require thermotolerant and alkaline cellulases. (AU)

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
FAPESP's process: 13/13309-0 - Studies of the structural and functional behavior of enzymes evolutionarily specialized in the degradation of plant biomass with potential biotechnological applications
Grantee:Mário Tyago Murakami
Support type: Regular Research 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: 09/08312-6 - Functional and structural investigations of the molecular mechanisms involved in signaling, regulation and activation of Class V myosins
Grantee:Mário Tyago Murakami
Support type: Regular Research Grants
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