Title
Fibril Formation from Pea Protein and Subsequent Gel Formation
Author
Munialo, XC.D.
Martin, A.H.
van der Linden, E.
de Jongh, H.H.J.
Publication year
2014
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 β-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.
Subject
Life
FI - Functional Ingredients
ELSS - Earth, Life and Social Sciences
Food and Nutrition
Nutrition
Healthy Living
Pea protein
Fibril assembly
Fibrillar aggregates
Whey protein
Soy protein
Gel formation
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http://resolver.tudelft.nl/uuid:d779ea97-d9c9-4d1f-9ec0-4732b076542b
DOI
https://doi.org/10.1021/jf4055215
TNO identifier
492059
Source
Journal of Agricultural and Food Chemistry, 62, 2418-2427
Document type
article