Quantitative assessment of thermal denaturation of bovine α-lactalbumin via low-intensity ultrasound, HPLC, and DSC

Qin Wang, Alexander Tolkach, Ulrich Kulozik

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

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.

Original languageEnglish
Pages (from-to)6501-6506
Number of pages6
JournalJournal of agricultural and food chemistry
Volume54
Issue number18
DOIs
StatePublished - 6 Sep 2006

Keywords

  • DSC
  • Degree of aggregation
  • HPLC
  • Protein denaturation
  • Ultrasound
  • α-lactalbumin

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