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A modified hypothesis for the structure and rheology of glutelins

✍ Scribed by J. A. D. Ewart


Publisher
John Wiley and Sons
Year
1972
Tongue
English
Weight
770 KB
Volume
23
Category
Article
ISSN
0022-5142

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✦ Synopsis


Cereal storage proteins, it is suggested, are more tolerant of genetic mutations than other proteins. Evolutionary tendencies may have been towards decreasing the cystine content and increasing the content of amino acids which are easily synthesised, especially those which are rich in nitrogen. The appearance of stress in molecular structure so that an intrachain SS bond is no longer able to close, thus creating interchain linkages, may have led to the origin of the glutelins.

It is argued that a viscoelastic dough can be formed only if protein particles, which originate in the form of protein bodies, are able to form a continuous structure whether maintained by covalent bonds orland secondary forces.

The constituent polypeptide chains of glutelins could be joined in a linear or a branched mode. A number of difficulties arise if the branched model is used to explain the properties of dough at the molecular level. In attempting to reconcile fact and theory, it is speculated that polypeptide chains of wheat, rye and barley glutelins form linear concatenations with two disulphide bonds connecting each chain to the next: continuity of structure in their doughs depends on entanglement and interaction by secondary forces. The glutelin molecules of oats and maize are unable to form a continuous network, hence the absence of viscoelasticity from doughs of these cereals. Two reasons are suggested: more probably the molecules are highly cross-linked in the branched mode and are thus incapable of significant entanglement; or if the molecules were cross-linked in the linear mode, poor solubility would ensure that protein-protein contacts in protein bodies were maintained, thus preventing dispersal of the protein and subsequent molecular entanglement. The glutelin molecules of sorghum appear to be too small to create a network by molecular entanglement. The importance of the disulphide interchange reaction is thought to lie in stress relaxation, but not in the creation of a dough structure. It is suggested that SS groups in viscoelastic doughs are sterically protected except when exposed by stress and consequently stress relaxation by SS interchange tends to occur only when it is needed.


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