Influence of toasting oak wood on ellagitannin structures

Must clarification is an important step occurring just after grape extraction in the elaboration of white wine, consisting in a solid-liquid separation. Traditionally, low must turbidity, around 50-150 NTU, is generally reached in white winemaking in order to prevent reductive aromas and facilitating alcoholic fermentation. Alternatively, a higher turbidity (300 NTU or above) can be sought for reasons such as a better expression of grapes identity (terroir), or for getting a must matrix that could supposedly lead to wines having greater ageing potential.

In red wines, anthocyanins evolve during the wine-making process and ageing. They react with other compounds (such as vinylphenols, acetaldehyde, pyruvic acid…) to form a stable family of compounds called pyranoanthocyanins. Furthermore, the oxidation process can modify the anthocyanic profile of a red wine. It is also interesting to evaluate the occurrence of the different subclasses of pyranoanthocyanins and to characterize their chemical properties. The first objective of this study is to evaluate the occurrence of the different groups of pyranoanthocyanins in an oxidised Merlot wine by a centrifugal partition chromatography strategy. The second goal is to evaluate their relative impact in red wines from Bordeaux region by measuring their concentrations.

Despite the extensive research performed during the last decades, the multifactorial mechanism responsible for the white wine protein haze formation is not fully characterized. Herein, a new model is proposed, which is based on the experimental identification of sulfur dioxide as a major modulating factor inducing wine protein haze upon heating. As opposed to other reducing agents, such as 2-mercaptoethanol, dithiothreitol and tris(2-carboxyethyl)phosphine hydrochloride (TCEP), the addition of SO2 to must/wine upon heating cleaves intraprotein disulfide bonds, hinders thiol-disulfide exchange during protein interactions and can lead to the formation of novel inter/intraprotein disulfide bonds. Those are eventually responsible for wine protein aggregation which follows a nucleation-growth kinetic model as shown by dynamic light scattering [1].

Laboratório de Análisis del Aroma y Enologia (LAAE). Department of Analytical Chemistry, Faculty of Sciences, Universidad de Zaragoza, 50009, Zaragoza, Spain, During alcoholic fermentation, fusel (or Strecker) aldehydes are intermediates in the amino acid catabolism to form fusel alcohols following the Ehrlich Pathway (1). One of the main enzymes involved in this pathway is Alcohol Dehydrogenase (ADH), whose activity is highly strain dependent and determines the rate of conversion of aldehydes into fusel alcohols (2). This enzyme has a Zn2+ catalytic binding site, which suggests that the must Zn2+ levels will most likely influence the rate of reduction of aldehydes into alcohols. On the other hand, SO2 is commonly used in winemaking for its antiseptic and antioxidant properties.

Among nitrogen compounds included in white wines, the peptide fraction is certainly the least studied, however this fraction is quantitatively the most important (Feuillat, 1974). Existing studies concern the fraction below 1 kDa and only for white and sparkling wines (Bartolomé et al, 1997, Desportes et al 2000). In this report, we have developed methods to isolate peptides from reference white wines. Then, we have applied this methodology with bitter wine to answer a research question: is there a relation between peptides and the bitterness of white wine as for some cheese for example (Furtado, 1984)?