Fibril Formation from Pea Protein and Sesequent Gel Formation

C.D. Munialo, A.H. Martin, E. van der Linden, H.H.J. de Jongh

Research output: Contribution to journalArticleAcademicpeer-review

69 Citations (Scopus)

Abstract

The objective of this study was to characterize fibrillar aggregates made using pea proteins, to assemble formed fibrils into protein-based gels, and to study the rheological behavior of these gels. Micrometer-long fibrillar aggregates were observed after pea protein solutions had been heated for 20 h at pH 2.0. Following heating of pea proteins, it was observed that all of the proteins were hydrolyzed into peptides and that 50% of these peptides were assembled into fibrils. Changes on a structural level in pea proteins were studied using circular dichroism, transmission electron microscopy, and particle size analysis. During the fibril assembly process, an increase in aggregate size was observed, which coincided with an increase in thioflavin T binding, indicating the presence of ß-sheet aggregates. Fibrils made using pea proteins were more branched and curly. Gel formation of preformed fibrils was induced by slow acidification from pH 7.0 to a final pH of around pH 5.0. The ability of pea protein-based fibrillar gels to fracture during an amplitude sweep was comparable to those of soy protein and whey protein-based fibrillar gels, although gels prepared from fibrils made using pea protein and soy protein were weaker than those of whey protein. The findings show that fibrils can be prepared from pea protein, which can be incorporated into protein-based fibrillar gels.
Original languageEnglish
Pages (from-to)2418-2427
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number11
DOIs
Publication statusPublished - 2014

Keywords

  • beta-lactoglobulin gels
  • amyloid fibrils
  • ph 2.0
  • electrostatic interactions
  • functional-properties
  • circular-dichroism
  • globular-proteins
  • heat
  • gelation
  • behavior

Fingerprint

Dive into the research topics of 'Fibril Formation from Pea Protein and Sesequent Gel Formation'. Together they form a unique fingerprint.

Cite this