AOC valorization of terroir nuances at plot scale in Burgundy

Viral diseases are reported to cause several detrimental effects on grapevine. Among them, leafroll, due to single or mixed infection of GLRaV1 and GLRaV3, and rugose wood, associated to GVA, are considered the most widespread and dangerous.

In contrast to fruit and grape berry ripening, the biological processes causing ripening disorders are often much less understood, although shriveling disorders of fruits are manifold and contribute to yield losses and reduced fruit quality worldwide. Shrinking berries are a common feature for all shriveling disorders in grapevine although their timing of appearance during the berry ripening process and their underlying induction processes distinct them from each other. The sugar accumulation disorder Berry Shrivel (BS) is characterized by a suppression of sugar accumulation short after veraison resulting in berries low in sugar content and anthocyanins in berry skins, while the organic acid content is similar. Recent studies analyzed the biochemical, morphological and molecular processes affected in BS berries and linked early changes to the period of ripening onset [1,2].

AIM This work aims to investigate fluorescence spectroscopy as a tool to assess grape homogenates to discriminate between samples of varying maturities and to develop an index to objectively characterise the level of grape heterogeneity present in any given vineyard.

The UN Agenda 2030 for Sustainable Development, a global plan for a better future, requires actions.

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].