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1.
Foods ; 11(3)2022 Jan 31.
Article in English | MEDLINE | ID: mdl-35159565

ABSTRACT

Winemaking is a stressful procedure for yeast cells. The presence of high levels of carbohydrates at the beginning of the fermentation and the subsequent increase of ethanol levels alongside with other environmental factors force the cell to undergo a continuous adaptation process. Ideally, yeast strains should be able to adapt to this changing environment fast and they must be able to ferment at low temperatures with the highest possible fermentation rates. Additionally, the balanced utilization of glucose and fructose-the two major hexoses in grapes-is also important as any residual fructose may confers unwanted sweetness. As proteins, Msn2/4 are known to play pivotal roles in cell stress response, the question that arise regards the differentially cell response driven by specific point mutations in these two proteins, and the subsequent effects on alcoholic fermentation. Four different mutants in which serine residues have been replaced by alanine are studied in this paper. Our results indicate that substitution at position 533 of Msn4 protein (W_M4_533) significantly increases the fermentation rate even at low temperatures (12 °C), by lowering the fermentation's activation energy. Similar results but to a lesser extent were obtained by the S582A substitution in Msn2 protein. In addition, W_M4_533 seems to have a more balanced utilization of must hexoses. From the present work it is concluded that genetic modification Msn2/4 represents a promising procedure for shortening the fermentation time, even at low temperatures, which in many cases constitutes an important technological requirement.

2.
J Chromatogr A ; 1524: 169-178, 2017 Nov 17.
Article in English | MEDLINE | ID: mdl-28992988

ABSTRACT

This work focuses on the influences of surfactants on the activity coefficients, γ, of methanol in binary mixtures with water, as well as on the mass transfer coefficients, kc, for the evaporation of methanol, which is a ubiquitous component in the troposphere, from mixtures of methanol with water at various surfactant's and methanol's concentrations. The technique used is the Reversed-Flow Gas Chromatography (R.F.G.C.), a version of Inverse Gas Chromatography, which allows determining both parameters by performing only one experiment for the kc parameter and two experiments for the γ parameter. The kc and γ values decrease in the presence of the three surfactants used (CTAB, SDS, TRITON X-100) at all methanol's and surfactant's concentrations. The decrease in the methanol's molar fraction, at constant number of surfactant films leads to a decrease in the kc and γ values, while the decrease in the surfactant's concentration, at constant methanol's molar fraction leads to an increase in both the kc and γ parameters. Mass transfer coefficients for the evaporation of methanol at the surfactant films, are also calculated which are approximately between 4 and 5 orders of magnitude larger than the corresponding mass transfer coefficients at the liquid films. Finally, thicknesses of the boundary layer of methanol in the mixtures of methanol with water were determined. The quantities found are compared with those given in the literature or calculated theoretically using various empirical equations. The precision of the R.F.G.C. method for measuring γ and kc parameters is approximately high (94.3-98.0%), showing that R.F.G.C. can be used with success not only for the thermodynamic study of solutions, but also for the interphase transport.


Subject(s)
Chemistry Techniques, Analytical/methods , Chromatography, Gas , Methanol/chemistry , Surface-Active Agents/chemistry , Water/chemistry
3.
J Chromatogr A ; 1305: 221-9, 2013 Aug 30.
Article in English | MEDLINE | ID: mdl-23899382

ABSTRACT

Milk proteins are able to facilitate the formation and stabilization of oil droplets in food emulsions. This study employed Sedimentation Field-Flow Fractionation (SdFFF) to monitor changes in particle size distribution of freshly prepared emulsions with varying weight contributions of sodium caseinate (SC) and whey protein concentrate (WPC). The effect of the addition of Tween 80 (T) on the initial droplet size was also investigated. The results indicated that emulsifying ability follows the order Tween 80>WPC>SC, with corresponding weight average droplet diameter of 0.319, 0.487 and 0.531µm respectively, when each of the above emulsifiers was used solely. The stability of sodium caseinate emulsions was studied at 30.5 and 80.0°C by measuring the particle size distribution for a period of 70h. Emulsions withstood the temperatures and exhibited an initial increase in particle size distribution caused by heat-induced droplet aggregation, followed by a decrease to approximately the initial droplet size. The rate of droplet aggregation depends on the severity of thermal processing, as revealed by the kinetics of particle aggregation during aging at different temperatures. Comparison of the experimental rate constants found from SdFFF, with those determined theoretically gives invaluable information about the oil droplet stability and the aggregation mechanism. Based on the proposed mechanistic scheme various physicochemical quantities, which are very important in explaining the stability of oil-in-water emulsions, were determined. Finally, the advantages of SdFFF in studying the aggregation of the oil-in-water droplets, in comparison with other methods used for the same purpose, are discussed.


Subject(s)
Emulsions , Fractionation, Field Flow , Milk Proteins/chemistry , Surface-Active Agents/chemistry , Kinetics , Microscopy, Electron, Scanning , Oils/chemistry , Particle Size , Water/chemistry
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