Title
Characterization of Pea Vicilin. 2. Consequences of Compositional Heterogeneity on Heat-Induced Gelation Behavior
Author
O'Kane, F.E.
Happe, R.P.
Vereijken, J.M.
Gruppen, H.
van Boekel, M.A.J.S.
TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
Publication year
2004
Abstract
The gelling characteristics of two vicilin fractions from pea (Pisum sativum L.) were compared over a range of pH and salt conditions after preliminary results showed that despite having equal opportunity to unfold, and expose hydrophobic residues, they had different minimum gelling concentrations (at pH 7.6). Furthermore, at this pH one fraction formed turbid gels and the other formed transparent gels. The fraction that formed transparent gels contained a substantial amount of the 70 kDa α-subunits of vicilin, and thus it was hypothesized that the highly charged N-terminal extension region on these 70 kDa subunits hinders gelation of this vicilin fraction at pH 7.6 and I = 0.2 due to repulsion of the net negative charge. The experiments designed to test this hypothesis are presented and discussed in this paper and prove that the hypothesis was true, which offers the possibility to control or modify the gelation behavior of vicilin on the basis of information of its subunit composition.
Subject
Nutrition
Food technology
Aggregation
Gelation
Heterogeneity
N-terminal extension region
Pisum
Storage proteins
Turbid and transparent gels
vicilin
Alpha chain
Amino terminal sequence
Concentration response
Gelation
Heat
Hydrophobicity
Nonhuman
Pea
PH
Protein analysis
Protein folding
Turbidity
Gels
Heat
Hydrogen-Ion Concentration
Peas
Plant Proteins
Protein Folding
Sodium Chloride
Pisum
Pisum sativum
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DOI
https://doi.org/10.1021/jf035105a
TNO identifier
237769
ISSN
0021-8561
Source
Journal of Agricultural and Food Chemistry, 52 (10), 3149-3154
Document type
article