Prediction of the production kinetics of the main fermentative aromas in alcoholic fermentation

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].

The Ability of PVPP (Polyvinylpolypyrrolidone), PVP-DEGMA-TAIC (copolimerization of N-vinyl-2-pyrrolidinone with ethylene glycol dimethacrylate and triallyl isocyanurate) and PAEGDMA
(poly(acrylamide-co-ethylene glycol dimethacrylate)) polymers was tested as removal agents for Fumonisin B1 (FB1) and Fumonisin B2 (FB2) from model solutions and red wine. The polymers removal capacity was checked at three different resident times (2, 8 and 24 hours of contact time between the polymer and the sample), showing no differences in the percentage of FB1 and FB2 removal. Then, different polymer concentrations (1, 5 and 10 mg mL-1) were tested in model solution with and without phenolics (i.e. gallic acid and 4-methylcatechol).

The use of glutathione (GSH) in winemaking has been legitimated recently, according to OIV resolutions OENO 445-2015 and OENO 446-2015 a maximum dose of 20 mg/L is now allowed to use in must and wine. Several studies have proven the benefits of GSH, predominantly in Sauvignon blanc. Thus, oxidative coloration of must and wine is limited, aroma compounds such as volatile thiols are preserved, and the development of ageing flavors such as sotolon and 2-aminoacetophenone is impeded. The protective effect may be explained by the high affinity of GSH to bind o-quinones which are formed during phenolic oxidation and which are known to initiate browning and other oxidative changes. Some researchers have proposed the hydroxycinnamic acid to GSH ratio (HGR) as an indicator of oxidation susceptibility of must and could show that lower ratios yielded lighter musts.

Chitosan is a polysaccharide produced from the deacetylation of chitin extracted from crustaceous and fungi. In winemaking chitosan is mainly used in the clarification of grape juice and wine, stabilization of white wines, removal of metals and to prevent wine spoilage by undesired microorganisms. The addition of chitosan to model wine systems was able to retard browning, reduce levels of metallic ions (Fe and Cu) and to protect varietal thiols due to its antiradical activity1. The present experiment was planned in order to evaluate the use of chitosan as a secondary antioxidant at three different stages of Sauvignon blanc fermentation and winemaking. Sauvignon blanc juices from three different locations were obtained at a commercial winery in Marlborough, New Zealand. One lots of grapes was collected from a receival bin and pressed into juice with a water-bag press, and a further juice sample was collected from a commercial pressing operation. Chitosan (1 g/L, low molecular weight, 75 – 85% deacetylated) was added to the juice after pressing, after cold settling, after fermentation, or at all these stages. Controls without any chitosan additions were also prepared.

The interactions among aromatic compounds and proteins is an important issue for the quality of foods and beverages. In wine, the loss of flavor after vinification is associated to bentonite treatment and this effect can be the result of the removal of aroma compounds which are bound wine proteins. This phenomenon was recently demonstrated for long chain fatty acids and their ethyl esters (1). Since these latter compounds are spectroscopically silent, their association with proteins is not easy to measure.