Artículos de revistas
The Coptotermes Gestroi Aldo-keto Reductase: A Multipurpose Enzyme For Biorefinery Applications
Registro en:
Biotechnology For Biofuels. Biomed Central Ltd, v. 10, p. , 2017.
1754-6834
WOS:000393842400004
10.1186/s13068-016-0688-6
Autor
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
Institución
Resumen
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) 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. 10 FAPESP [2014/20576-7, 2011/2977-3, 2012/20549-4, 08/58037-9, 2013/06336-0, 2014/04105-4] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)