English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/164319
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
DC FieldValueLanguage
dc.contributor.authorMéndez-Líter, Juan A.-
dc.contributor.authorEugenio, Laura I. de-
dc.contributor.authorPrieto, Alicia-
dc.contributor.authorMartínez, María Jesús-
dc.date.accessioned2018-04-29T03:36:29Z-
dc.date.available2018-04-29T03:36:29Z-
dc.date.issued2018-04-27-
dc.identifier.citationBiotechnology for Biofuels 11(1): 123 (2018)-
dc.identifier.urihttp://hdl.handle.net/10261/164319-
dc.description.abstractAbstract Background In the last years, the most outstanding trend for obtaining high added-value components and second-generation (2G) biofuels consisted on exploitation of plant biomass. But recently, 3G biofuels, based in algae biomass, have emerged as a great alternative for production of energy. Results In this work, a versatile β-glucosidase from the ascomycete fungus Talaromyces amestolkiae has been purified, characterized, and heterologously expressed. The synthesis of this β-glucosidase (BGL-3) was not induced by cellulose, and the presence of a specific carbon source is not required for its production, which is uncommon for β-glucosidases. BGL-3, which was obtained from a basal medium with glucose as carbon source, was profusely secreted under carbon starvation conditions, which was corroborated by qRT-PCR assays. BGL-3 was purified from T. amestolkiae cultures in one step, and biochemically characterized. The enzyme showed high thermal stability, and very high efficiency on pNPG (Km of 0.14 mM and Vmax of 381.1 U/mg), cellobiose (Km of 0.48 mM and Vmax of 447.1 U/mg), and other cello-oligosaccharides. Surprisingly, it also showed remarkable ability to hydrolyze laminarin, a β-1,3-glucan present in algae. The recombinant enzyme, obtained in the yeast Pichia pastoris, exhibited kinetic and physicochemical properties similar to those found for the native protein. Enzyme efficiency was examined in wheat straw saccharification processes, in which BGL-3 worked better supplementing Celluclast 1.5L than the commercial cellulase cocktail N-50010. Besides, BGL-3 hydrolyzed laminarin more efficiently than a commercial laminarinase. Conclusions A very efficient 1,4-β-glucosidase, which also showed activity over 1,3-β-glucose bonds, has been produced, purified, and characterized. This is the first report of such versatility in a 1,4-β-glucosidase. The application of this enzyme for saccharification of wheat straw and laminarin and its comparison with commercial enzymes suggest that it could be an interesting tool for the production of 2G and 3G biofuels.-
dc.description.sponsorshipThe authors thank the Proteomics and Genomics facility at CIB, Novozymes, for providing the commercial cocktails, and Abengoa for supplying pretreated wheat straw. J.A. Méndez thanks its fellowship to Tatiana Pérez de Guzmán el Bueno Foundation. We acknowledge support of the publication fee by the CSIC Open Access Publication Support Initiative through its Unit of Informa‑ tion Resources for Research (URICI). We are indebted to A. Serrano for her help using protein structure software.-
dc.publisherBioMed Central-
dc.relationS2013/MAE-2907-
dc.relationMINECO/ICTI2013-2016/RTC-2014-1777-3-
dc.relationMINECO/ICTI2013-2016/BIO2015-68387-R-
dc.relation.isversionofPublisher's version-
dc.rightsopenAccess-
dc.titleThe β-glucosidase secreted by Talaromyces amestolkiae under carbon starvation: a versatile catalyst for biofuel production from plant and algal biomass-
dc.typeartículo-
dc.identifier.doi10.1186/s13068-018-1125-9-
dc.relation.publisherversionhttps://doi.org/10.1186/s13068-018-1125-9-
dc.date.updated2018-04-29T03:36:30Z-
dc.language.rfc3066en-
dc.rights.holderThe Author(s)-
dc.rights.licensehttp://creativecommons.org/licenses/by/4.0/-
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)-
dc.contributor.funderEuropean Commission-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderComunidad de Madrid-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
13068_2018_Article_1125.pdf1,24 MBAdobe PDFThumbnail
View/Open
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.