Abstract
The degree of irreversible aggregation and the aggregation velocity constant of α-lactalbumin (α-la) were determined by three methods based on different principles: low-intensity ultrasound as a novel method for this purpose, DSC, and HPLC. The denaturation process of α-la causes a decrease in the ultrasonic velocity due to the conformation change of α-la molecules. This decrease is a function of the concentration of native α-la in the sample. A linear correlation was found between the degree of aggregation of α-la determined by these three methods. There is no significant difference between the aggregation velocity constants determined by the three methods. The results show that the ultrasonic method is capable of quantifying the degree of aggregation of a protein, offering an alternative method.
Originalsprache | Englisch |
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Seiten (von - bis) | 6501-6506 |
Seitenumfang | 6 |
Fachzeitschrift | Journal of agricultural and food chemistry |
Jahrgang | 54 |
Ausgabenummer | 18 |
DOIs | |
Publikationsstatus | Veröffentlicht - 6 Sept. 2006 |