Can the use of rootstocks enhance terroir?

There are currently enzyme preparations on the market with specific protease activities capable of degrading unstable must proteins and preventing turbidity in white and rosé wines. The main drawback is the need to heat the must at 75ºc for 1-2 minutes to denature the proteins and facilitate enzyme action.

Volatile thiols contribute largely to the organoleptic characteristics and typicity of Sauvignon blanc wines. Among this family of odorous compounds, 3-sulfanylhexan-1-ol (3SH) and 4-methyl-4-sulfanylpentan-2-one (4MSP) have a major impact on wine flavor. These thiols are formed during alcoholic fermentation by the yeast from odorless and non-volatile precursors found in the berry and the must. The effect of vine nitrogen status on 3SH and 4MSP in Sauvignon blanc wine and on the glutathionylated and cysteinylated precursors of 3SH (Glut-3SH and Cys-3SH) was investigated in this study.

Water stress triggers functional compartmentalization in grapevines, influencing how resources are allocated to different plant organs.

DNA-binding proteins play a pivotal role in critical cellular processes such as DNA replication, transcription, recombination, repair, and other essential activities. Consequently, investigating the interactions between DNA and proteins is of paramount importance to gain insights into these fundamental cellular mechanisms. Several methodologies have been devised to uncover DNA-protein interactions, which can be broadly categorized into two approaches. The “protein-centered” approach focuses on identifying the DNA sequences bound by a specific transcription factor or a set of TFs. Techniques falling within this category include chromatin immunoprecipitation, and protein-binding microarrays.

This paper presents the results of an agroclimatic study of the viticulture area called DOC Monreale (Pa), Italy, which was carried out with the aim to supply a working instrument supporting viticulture planning.