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A novel feruloyl esterase from Oenococcus oeni for the improvement of wine quality

AutorSantamaría, Laura; Esteban-Torres, María ; Reverón, Inés ; Barcenilla Moraleda, José María ; Muñoz, Rosario ; Rivas, Blanca de las
Palabras claveFeruloyl esterase
Oenococcus oeni
Fecha de publicación2017
CitaciónBioMicroWorld 2017
ResumenAlthough malolactic fermentation is the main transformation carried out by Oenococcus oeni during vinification, it is not the only one. There are other metabolic reactions that can have positive effects on quality of wine as a myriad of other changes occur to complete the transformation of grape juice to wine. Many of these processes involved the action of enzymes. Such enzymes can be originated from several sources that included the grape microbiota, the inoculated microbes, or microbes associated with winery equipment. To improve wine quality and complexity, efforts have often been centered on desirable enzymatic activities, such as esterases from microorganisms encountered during vinification. Esters are flavour compounds that are extremely important for the flavour profile of wines, e.g. esters are responsible for the desirable, fruity aroma of young wines. O. oeni is frequently utilized as a starter culture to promote malolactic conversion. Therefore O. oeni enzymes are highly relevant on wine aroma. Among the enzymes annotated on the O.oeni PSU-1 genome, a gene encoding a putative esterase was found. This gene was cloned and expressed in Escherichia coli, and the corresponding protein was hiperproduced and biochemically characterized. The protein showed esterase activity on esters derived from phenolic acids. It showed feruloyl esterase activity as well as esterase activity on esters derived from hydroxybenzoic acids (e.g., gallic acid). The protein exhibited optimum temperature and pH for activity at 40ºC and 5.0, respectively. Furthermore, the protein kept 80% of its maximal activity after 20 h incubation at 20ºC, 30ºC and 37ºC. The effect of wine compounds on esterase activity was studied. From the compounds assayed, 20 % ethanol inhibited esterase activity. The obtained results indicated that the esterase from O. oeni could be an adequate esterase enzyme to be used during vinification to flavor enhancement of wine.
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.
Aparece en las colecciones: (ICTAN) Comunicaciones congresos
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