Characterization of Pea Vicilin. 2. Consequences of Compositional Heterogeneity on Heat-Induced Gelation Behavior
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- 作者：Francesca E. O'Kane ; Randolph P. Happe ; Johan M. Vereijken ; Harry Gruppen ; and Martinus A. J. S. van Boekel
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2004
- 出版时间：May 19, 2004
- 年：2004
- 卷：52
- 期：10
- 页码：3149 - 3154
- 全文大小：96K
- 年卷期：v.52,no.10(May 19, 2004)
- ISSN：1520-5118
文摘
The gelling characteristics of two vicilin fractions from pea (Pisum sativum L.) were compared overa range of pH and salt conditions after preliminary results showed that despite having equal opportunityto unfold, and expose hydrophobic residues, they had different minimum gelling concentrations (atpH 7.6). Furthermore, at this pH one fraction formed turbid gels and the other formed transparentgels. The fraction that formed transparent gels contained a substantial amount of the 70 kDa 
-subunitsof vicilin, and thus it was hypothesized that the highly charged N-terminal extension region on these70 kDa subunits hinders gelation of this vicilin fraction at pH 7.6 and I = 0.2 due to repulsion of thenet negative charge. The experiments designed to test this hypothesis are presented and discussedin this paper and prove that the hypothesis was true, which offers the possibility to control or modifythe gelation behavior of vicilin on the basis of information of its subunit composition.Keywords: Pisum; storage proteins; heterogeneity; N-terminal extension region; aggregation; gelation;turbid and transparent gels
-subunitsof vicilin, and thus it was hypothesized that the highly charged N-terminal extension region on these70 kDa subunits hinders gelation of this vicilin fraction at pH 7.6 and I = 0.2 due to repulsion of thenet negative charge. The experiments designed to test this hypothesis are presented and discussedin this paper and prove that the hypothesis was true, which offers the possibility to control or modifythe gelation behavior of vicilin on the basis of information of its subunit composition.Keywords: Pisum; storage proteins; heterogeneity; N-terminal extension region; aggregation; gelation;turbid and transparent gels