Kafirin structure and functionality

Belton, Peter, Delgadillo, I, Halford, N and Shewry, P (2006) Kafirin structure and functionality. Journal of Cereal Science, 44 (3). pp. 272-286.

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Abstract

The structural and functional properties of kafirins are reviewed. Three classes of kafirin: the a, ß and ? forms have been identified at the protein level and one, the d, has been identified only at the gene and transcript levels. All forms show high homology with the equivalent zein proteins. By analogy with the zeins it is believed that the a-kafirins probably have an extended hairpin structure in solution, comprising elements of a-helix, ß-sheet and turns folded back on itself. Kafirins are the most hydrophobic of the prolamins as shown by their solubility, and calculated hydration free energies. The proteins exhibit extensive cross-linking by disulphide bonds and on cooking form indigestible aggregates which are not solubilised by reduction of disulphide bonds. In spite of continuing studies, the reasons for the low digestibility of the protein remain uncertain and there may be several factors involved. Other research has shown that kafirins may have non-food uses and may be used to form films.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Depositing User:	Rachel Smith
Date Deposited:	07 Mar 2011 16:55
Last Modified:	24 Sep 2024 09:47
URI:	https://ueaeprints.uea.ac.uk/id/eprint/21259
DOI:	10.1016/j.jcs.2006.05.004

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