The Critical Aggregation Concentration of ß-Lactoglobulin-Based Fibril Formation

A. Kroes-Nijboer, P. Venema, J. Bouman, E. van der Linden

Research output: Contribution to journalArticleAcademicpeer-review

35 Citations (Scopus)

Abstract

The critical aggregation concentration (CAC) for fibril formation of ß-lactoglobulin (ß-lg) at pH 2 was determined at 343, 353, 358, 363, and 383 K using a Thioflavin T assay and was approximately 0.16 wt%. The accuracy of the CAC was increased by measuring the conversion into fibrils at different stirring speeds. The corresponding binding energy per mol, as determined from the CAC, was 13 RT (~40 kJ mol¿1) for the measured temperature range. The fact that the CAC was independent of temperature within the experimental error indicates that the fibril formation of ß-lg at pH 2 and the measured temperature range is an entropy-driven process.
Original languageEnglish
Pages (from-to)59-63
JournalFood Biophysics
Volume4
Issue number2
DOIs
Publication statusPublished - 2009

Keywords

  • heat-induced denaturation
  • amyloid fibrils
  • globular-proteins
  • whey-protein
  • ionic-strength
  • low ph
  • gels
  • gelation
  • ovalbumin
  • lysozyme

Fingerprint Dive into the research topics of 'The Critical Aggregation Concentration of ß-Lactoglobulin-Based Fibril Formation'. Together they form a unique fingerprint.

Cite this