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The present review aims to show the state of the art of oxidation mechanisms occurring especially in white wines by taking into account knowledge from different fields in relation to the subject. It is therefore divided into three main parts. First, the mechanisms of oxidation relevant to white wine are discussed in the light of recent scientific literature. Next, the phenomenon of oxygen solubility in wine during the winemaking process, and in particular during bottling is stated theoretically as well as practically. Finally, the aspect of wine conservation after bottling is examined with respect to mass transfers which may occur through the closure, with a special emphasis on cork. Currently, specific physico-chemical properties still make cork closures the most important closure type used for the wine market, and especially for high quality wines. This final section will also include a review of studies performed on this subject, which have been analyzed in detail from a theoretical mass transfer point of view, in order to assess the extent to which the proposed scientific tools and the observed tendencies are relevant to progress in the understanding of the impact of this parameter on the behavior of a wine. [ABSTRACT FROM AUTHOR]

We report here for the first time a complete thermodynamic study of water vapor adsorption on crude cork powder and plate. Adsorption-desorption isotherms were accurately measured by thermogravimetry at 283, 298, and 313 K in a large range of relative pressure. Adsorption enthalpies were determined by calorimetry as a function of loading. Adsorption-desorption isotherms exhibit a hysteresis due to the swelling of the material. The influence of the presence of lenticels on the adsorption properties of cork is found to be negligible. A detailed analysis and interpretation of adsorption data allow proposal of an adsorption mechanism in two steps. (i) First, water adsorbs on hydrophilic sites constituted by hydroxyl and methoxyl groups. (ii) Then water adsorption continues by clusters formation around the hydrophilic sites.

Synthetic alamethicin analogs, in which all Aib residues had been replaced by Leu (L2) then proline 14 replaced by an alanine (L5), were studied in SDS micelles using circular dichroism and NMR spectroscopy. Nuclear Overhauser effects were used as constraints for molecular modelling. The structures determined for both peptides in SDS micelles were compared with those previously obtained in methanol in order to establish a secondary structure/ionophore activity relationship. Our results indicated that a shortening of peptide helices could be responsible for the observed decrease in ion channel lifetimes. However, the length of helices may not by itself explain the drastic destabilization of channels when Pro14 of alamethicin is replaced by Ala in L5. Indeed analysis of the helical wheel of L5 reveals heterogeneity in the amphipathicity depending on the medium. Thus, loss of amphipathicity seems to underly the observed destabilization of channels.

Due to the bend introduced by proline 14 in the conformation of alamethicin (AcUPUAUAQUVUGLUPV UUEQFol), the role of this residue was assumed essential in the barrel-stave model for voltage-gated ion channels. Taking advantage of a previous synthetic alamethicin analogue (L2), in which all eight alpha-aminoisobutyric (U) were replaced by leucines (AcLPLALAQLV LGLLPV LLEQFol), another analogue (L5) was synthesized in order to test the effects of proline-14 substitution by an alanine (AcLPLALAQLVLGLLPVLLEQFol). Previous conductance experiments showed that both high voltage dependence and multistate behavior were conserved. In order to complement these functional results, a conformational study of L5 has been undertaken and compared to L2 using CD, high field nmr, and molecular dynamics. Results show that L5 presents a better ordered structure than L2 particularly in the region of the substitution and in the C-terminal part. These results are discussed as regards the previous hypothesis of the nonessential character of helix bending for the gating of voltage-dependent ion channels.

Alamethicin, a 20-residue peptaibol, induces voltage-dependent ion channels in lipid bilayers according to the barrel-stave model. A synthetic analogue (L2) in which all Aib were replaced by Leu shows a conductance behaviour similar to alamethicin, but channel lifetimes are drastically reduced. Among several hypotheses, a different conformation for L2 might be responsible for this phenomenon by increasing the alpha-helical content (alamethicin presents some 3.0(10)-helical parts) and thus decreasing the length of the transmembrane part. A conformational study of L2 was undertaken using FTIR, CD and NMR spectroscopy, and the secondary structure was compared with alamethicin. These techniques showed an enhanced predominant helical structure as compared to alamethicin. Moreover, the NOE pattern showed an exclusively alpha-helical conformation, resulting in a smaller length of the L2 peptide. This shortening somewhat impedes the complete crossing of the membrane, and could then explain the reduction of its ion-channel lifetimes.