Protein–Peptide Interaction: Study of Heat-Induced Aggregation and Gelation of ß-Lactoglobulin in the Presence of Two Peptides from Its Own Hydrolysate

H.A. Kosters, P.A. Wierenga, R.J. de Vries, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

8 Citations (Scopus)

Abstract

Two peptides, [f135–158] and [f135–162]-SH, were used to study the binding of the peptides to native ß-lactolobulin, as well as the subsequent effects on aggregation and gelation of ß-lactoglobulin. The binding of the peptide [f135–158] to ß-lactoglobulin at room temperature was confirmed by SELDI-TOF-MS. It was further illustrated by increased turbidity of mixed solutions of peptide and protein (at pH 7), indicating association of proteins and peptides in larger complexes. At pH below the isoelectric point of the protein, the presence of peptides did not lead to an increased turbidity, showing the absence of complexation. The protein–peptide complexes formed at pH 7 were found to dissociate directly upon heating. After prolonged heating, extensive aggregation was observed, whereas no aggregation was seen for the pure protein or pure peptide solutions. The presence of the free sulfhydryl group in [f135–162]-SH resulted in a 10 times increase in the amount of aggregation of ß-lactoglobulin upon heating, illustrating the additional effect of the free sulfhydryl group. Subsequent studies on the gel strength of heat-induced gels also showed a clear difference between these two peptides. The replacement of additional ß-lactoglobulin by [f135–158] resulted in a decrease in gel strength, whereas replacement by peptide [f135–162]-SH increased gel strength.
Original languageEnglish
Pages (from-to)4218-4225
JournalJournal of Agricultural and Food Chemistry
Volume61
Issue number18
DOIs
Publication statusPublished - 2013

Keywords

  • rheological properties
  • alpha-lactalbumin
  • gels
  • isolate
  • acid
  • ovalbumin
  • fractions
  • soy

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