Relation of β-lactoglobulin - Sodium polypectate aggregation to bulk macromolecular concentration

Embola E. Ndi, B. G. Swanson, A. K. Dunker, L. O. Luedecke

Research output: Contribution to journalArticle

6 Scopus citations


Aggregation of β-Lactoglobulin (β-Lg) solutions, with and without sodium polypectate (SPP), was investigated at pH 6.5 and 3.5 by turbidity measurements and gel permeation chromatography during heating at 1°C/min. The ratio of β-Lg:SPP was maintained at 10:1. At pH 6.5, the transition temperature of β-Lg aggregation decreased linearly with the logarithm of β-Lg concentration. Irrespective of β-Lg concentration, SPP did not affect the rate of β-Lg aggregation during heating at pH 6.5. However, SPP influenced the formation of high-molecular-weight (HMW) β-Lg aggregates during heating at pH 6.5 was related to bulk macromolecular concentration. No thermal aggregation transitions were detected for β-Lg solutions at pH 3.5. SPP interacted with β-Lg at pH 3.5 to form a complex that precipitated on heating.

Original languageEnglish (US)
Pages (from-to)69-73
Number of pages5
JournalJournal of Food Science
Issue number1
StatePublished - Jan 1 1996
Externally publishedYes


  • Sodium polypectate
  • Thermal aggregation
  • Transition temperature
  • β-lactoglobulin

ASJC Scopus subject areas

  • Food Science

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