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

The Coptotermes gestroi aldo-keto reductase: a multipurpose enzyme for biorefinery applications

Full text
Show less -
Tramontina, Robson ; Franco Cairo, Joao Paulo L. ; Liberato, Marcelo V. ; Mandelli, Fernanda ; Sousa, Amanda ; Santos, Samantha ; Rabelo, Sarita Candida ; Campos, Bruna ; Ienczak, Jaciane ; Ruller, Roberto ; Damasio, Andre R. L. ; Squina, Fabio Marcio
Total Authors: 12
Document type: Journal article
Web of Science Citations: 6

Background: In nature, termites can be considered as a model biological system for biofuel research based on their remarkable efficiency for lignocellulosic biomass conversion. Redox enzymes are of interest in second-generation ethanol production because they promote synergic enzymatic activity with classical hydrolases for lignocellulose saccharification and inactivate fermentation inhibitory compounds produced after lignocellulose pretreatment steps. Results: In the present study, the biochemical and structural characteristics of the Coptotermes gestroi aldo-keto reductase (CgAKR-1) were comprehensively investigated. CgAKR-1 displayed major structural differences compared with others AKRs, including the differences in the amino acid composition of the substrate-binding site, providing basis for classification as a founding member of a new AKR subfamily (family AKR1 I). Immunolocalization assays with anti-CgAKR-1 antibodies resulted in strong fluorescence in the salivary gland, proventriculus, and foregut. CgAKR-1 supplementation caused a 32% reduction in phenolic aldehydes, such as furfural, which act as fermentation inhibitors of hemicellulosic hydrolysates, and improved ethanol fermentation by the xylose-fermenting yeast Scheffersomyces stipitis by 45%. We observed synergistic enzymatic interactions between CgAKR-1 and commercial cellulosic cocktail for sugarcane bagasse saccharification, with a maximum synergism degree of 2.17 for sugar release. Our data indicated that additive enzymatic activity could be mediated by reactive oxygen species because CgAKR-1 could produce hydrogen peroxide. Conclusion: In summary, we identified the founding member of an AKRI subfamily with a potential role in the termite digestome. CgAKR-1 was found to be a multipurpose enzyme with potential biotechnological applications. The present work provided a basis for the development and application of integrative and multipurpose enzymes in the bioethanol production chain. (AU)

FAPESP's process: 12/20549-4 - Secretion of heterologous glycoproteins in Aspergillus: effect of glycosylation pattern in functional parameters of glycosyl hydrolases
Grantee:André Ricardo de Lima Damasio
Support type: Program for Research on Bioenergy (BIOEN) - Young Investigators Grants
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: 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: 13/06336-0 - Study of the Molecular Basis of Carbohydrate Binding Modules (CBMs) from Metagenomic Screenings
Grantee:Bruna Medéia de Campos
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 14/20576-7 - Characterization of auxiliary (redox) enzymes from the termite Coptotermes gestroi that cooperate with glycolytic hydrolases
Grantee:Robson Tramontina
Support type: Scholarships in Brazil - Master