Effects of ethanol on structure and solubility of potato proteins and the effects of its presence during the preparation of a protein isolate
article
In this study, a protein isolate with a high solubility at neutral pH was prepared from industrial potato juice by precipitation at pH 5 in the presence of ethanol. The effects of ethanol itself and the effects of its presence during precipitation on the properties of various potato protein fractions were examined. The presence of ethanol significantly reduced the denaturation temperature of potato proteins, indicating that the preparation of this potato protein isolate should be performed at low temperature in order to retain a high solubility. In the presence of ethanol, the thermal unfolding of the tertiary and the secondary structure of patatin was shown to be almost completely independent. Even at 4 °C, precipitation of potato proteins in the presence of ethanol induced significant conformational changes. These changes did, however, only result in minor changes in the solubility of the potato protein fractions as a function of pH and heat treatment temperature.
Topics
Circular dichroismDifferential scanning calorimetryEthanolPatatinPotatoProtease inhibitorsProteinsSolanum tuberosumSolubilityStructural stabilityAlcoholCarboxylesterasePatatinVegetable proteinPatatin protein, Solanum tuberosumChemistryCircular dichroismConformational transitionDifferential scanning calorimetryHeatHeat treatmentLow temperatureNonhumanOsmolarityPHPotatoPrecipitationProtein conformationProtein denaturationProtein isolationProtein structureSolubilityTemperatureIsolation and purificationSolanum tuberosumTuberosumCalorimetry, Differential ScanningCarboxylic Ester HydrolasesCircular DichroismEthanolHeatHydrogen-Ion ConcentrationOsmolar ConcentrationPlant ProteinsPrecipitationProtein ConformationProtein DenaturationSolanum tuberosumSolubilityTemperature
TNO Identifier
72686
Source
Journal of Agricultural and Food Chemistry, 50, pp. 2947-2956.
Pages
2947-2956
Files
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