English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/172015
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Título

Biochemical characterization of Lp_2777, a family 1 glycoside hydrolase from Lactoibacillus plantarum WCFS1

AutorPlaza-Vinuesa, Laura; González, G.; Rivas, Blanca de las ; Muñoz, Rosario
Palabras claveLactobacillus plantarum
GH1 family
Glycosidases
Olive
Fecha de publicación2017
CitaciónBioMicroWorld 2017
ResumenGlycoside hydrolases (GHs) have been organized into 114 families in the CAZy database (http://www.cazy.org) based on amino acid sequence similarities. Among these families, glycoside hydrolase family 1 (GH1) enzymes are important members which hydrolyze β-glycosidic linkages. Carbohydrates are the major energy source for Lactic acid bacteria (LABs) and their metabolism utilizes a variety of sugars present in the environment. Carbohydrate uptake mostly occurs through the phosphoenolpyruvate-dependent phosphotranferase system (PEP-PTS). In olive (Olea europea), the glucoside oleuropein is the main phenolic component. Oleuropein is present in leaves as well as in olive fruits and is related to the bitterness of olive oil. Lactobacillus plantarum is a lactic acid bacteria frequently found in the fermentation of plant-derived food products like olives. It has been described that L. plantarum is able to transform oleuropein to hydroxytyrosol, the compound responsible of olive oil healthy properties. In order to identify the enzymes involved in oleuropein transformation, L. plantarum WCFS1 was exposed to oleuropein and the changes in gene expression analyzed. The transcriptomic study revealed the induction of the lp_2777 gene, encoding a putative 6 phospho β-glucosidase. Therefore, the lp_2777 gene was cloned and the recombinant protein was hiperproduced, purified, and biochemically characterized. Substrate specificity was assayed against a library of 4-nitrophenyl synthetic glycosides. The results showed that Lp_2777, in spite that it not exhibited β-glucosidase activity, it was able to hydrolyze 4-nitrophenyl-β-Dglucopyranoside-6-P, and 4-nitrophenyl-β-D-galactopyranoside-6-P. In addition, Lp_2777 protein showed thermal stability. This study constitutes the first characterization of a GH1 glycosidase from Lactobacillus plantarum WCFS1.
DescripciónPóster presentado a la VII International Conference on Environmental Industrial and Applied Microbiology, celebrada en Madrid (España) del 18 al 20 de octubre de 2017.
URIhttp://hdl.handle.net/10261/172015
Aparece en las colecciones: (ICTAN) Comunicaciones congresos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Ponen12biochem.pdf257,65 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.