The effect of heat on pea ( Pisum sativum L) vicilin has been studied using differential scanning calorimetry (DSC), gel filtrtion chromatography and turbidimetry. By adjusting the variables of pII, ionic strength and protein concentration, two processes could be identified from the DSC thermograms: protein denaturation and protein aggregation. The results are discussed in terms of electrostatic and hydrophobic interactions. A mechanism for the thermal aggregation of pea vicilin is proposed.
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Bacon et al. (1989) studied this question.
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