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Saccharification of Brown Macroalgae Using an Arsenal of Recombinant Alginate Lyases: Potential Application in the Biorefinery Process
Indexado
WoS WOS:000448398800010
Scopus SCOPUS_ID:85065752663
DOI 10.4014/JMB.1805.05056
Año 2018
Tipo artículo de investigación

Citas Totales

Autores Afiliación Chile

Instituciones Chile

% Participación
Internacional

Autores
Afiliación Extranjera

Instituciones
Extranjeras


Abstract



Alginate lyases (endo and exo-lyases) are required for the degradation of alginate into its constituting monomers. Efficient bioethanol production and extraction of bioactives from brown algae requires intensive use of these enzymes. Nonetheless, there are few commercial alginate lyase preparations, and their costs make them unsuitable for large scale experiments. A recombinant expression protocol has been developed in this study for producing seven endo-lyases and three exo-lyases as soluble and highly active preparations. Saccharification of alginate using 21 different endo/exo-lyase combinations shows that there is complementary enzymatic activity between some of the endo/exo pairs. This is probably due to favorable matching of their substrate biases for the different glycosidic bonds in the alginate molecule. Therefore, selection of enzymes for the best saccharification results for a given biomass should be based on screens comprising both types of lyases. Additionally, different incubation temperatures, enzyme load ratios, and enzyme loading strategies were assessed using the best four enzyme combinations for treating Macrocystis pyrifera biomass. It was shown that 30 degrees C with a 1:3 endo/exo loading ratio was suitable for all four combinations. Moreover, simultaneous loading of endo-and exo-lyases at the beginning of the reaction allowed maximum alginate saccharification in half the time than when the exo-lyases were added sequentially.

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Disciplinas de Investigación



WOS
Biotechnology & Applied Microbiology
Microbiology
Scopus
Biotechnology
Applied Microbiology And Biotechnology
SciELO
Sin Disciplinas

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Publicaciones WoS (Ediciones: ISSHP, ISTP, AHCI, SSCI, SCI), Scopus, SciELO Chile.

Colaboración Institucional



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Autores - Afiliación



Ord. Autor Género Institución - País
1 GIMPEL-HENRIQUEZ, JAVIER ANDRES Hombre Universidad de Chile - Chile
2 Ravanal, Maria-Cristina Mujer Universidad de Chile - Chile
Universidad Austral de Chile - Chile
3 SALAZAR-GUERRERO, OSVALDO Mujer Universidad de Chile - Chile
4 LIENQUEO-CONTRERAS, MARIA ELENA Mujer Universidad de Chile - Chile
4 Elena Lienqueo, Ma. Mujer Universidad de Chile - Chile

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Financiamiento



Fuente
Comision Nacional de InvestigacionCientifica y Tecnologica CONICYT, Chile

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Agradecimientos



Agradecimiento
This work was supported by Comision Nacional de InvestigacionCientifica y Tecnologica CONICYT, Chile: [Grant AKA-ERNC 009 PROJECT] and [Centre for Biotechnology and Bioengineering, CEBIB FB-0001]. Our thanks to Dr. Julia Rossmanith, Dr. Hueseyin Besir, Dr. Arie Geerlof, and the Protein Expression and Purification Facility, EMBL, Heidelberg, for facilitating the Gateway expression vectors utilized in this study.

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