Effects of pH and heat treatments on the structure and solubility of potato proteins in different preparations.
The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 degrees C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature. It was concluded that either the dimeric protein patatin unfolds in its monomeric state or its monomers are loosely associated and unfold independently. Thermal unfolding of the protease inhibitors was correlated with a decrease in protease inhibitor activities and resulted in an ionic strength dependent loss of protein solubility. Potato proteins were soluble at neutral and strongly acidic pH values. The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin.
van Koningsveld
G A
GA
Centre for Protein Technology, TNO-WU, Wageningen, The Netherlands.
Gruppen
H
H
de Jongh
H H
HH
Wijngaards
G
G
van Boekel
M A
MA
Walstra
P
P
Voragen
A G
AG
D002152:Calorimetry, Differential Scanning; D002265:Carboxylic Ester Hydrolases / Q000032:analysis / Q000737:chemistry; D011232:Chemical Precipitation; D002942:Circular Dichroism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D015394:Molecular Structure; D009994:Osmolar Concentration; D010940:Plant Proteins / Q000032:analysis / Q000737:chemistry*; D011480:Protease Inhibitors / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011198:Solanum tuberosum / Q000737:chemistry*; D012995:Solubility
D010940:Plant Proteins; D011480:Protease Inhibitors; C043222:patatin protein, Solanum tuberosum; D002265:Carboxylic Ester Hydrolases