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primary prevention of coeliac disease - Associazione Italiana ...

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76<br />

GENETICALLY DETOXIFIED GRAINS<br />

molecular weight proteins. High-molecular weight proteins (x - and y-type subunits)<br />

comprise the HMW subunits <strong>of</strong> glutenins; glutamine, glycine, and proline represent<br />

70% <strong>of</strong> total residues. Medium-molecular weight group consists <strong>of</strong> w-gliadins; 80% <strong>of</strong><br />

the amino acids is due to glutamine, proline, and phenylalanine, but cysteine and<br />

methionine, i.e. sulphur containing amino acids, are almost absent. Low-molecular<br />

weight proteins consist <strong>of</strong> a-, b-, g-gliadins and LMW subunits <strong>of</strong> glutenins; they are<br />

rich in sulphur containing amino acids.<br />

Functional properties <strong>of</strong> gluten proteins<br />

Although the only known function <strong>of</strong> these proteins is to act as storage proteins, by<br />

releasing nitrogen for the germinating seed, their biochemistry structure has a crucial<br />

2,6<br />

role in providing the unique baking quality <strong>of</strong> wheat . Both LMW and HMW have not<br />

only intrachain but also interchain disulphide bonds allowing them to crosslink other<br />

glutenin and gliadin peptides, which results in the formation <strong>of</strong> beta-spirals. During the<br />

baking process, CO<br />

2<br />

is produced by yeast fermentation and is trapped in the beta-spiral<br />

three dimensional net. Glutenins spirals become extended but maintain the capacity to<br />

return to the colloid state. So, elasticity and cohesivity <strong>of</strong> the dough system are due to<br />

the cross-linked nature <strong>of</strong> the glutenin subunits, mainly the high molecular weight<br />

glutenins. On the other hand, soluble monomeric gliadins guarantee extensibility and<br />

viscosity to the dough (Fig. 1).<br />

Coeliac toxicity <strong>of</strong> gliadins and glutenins<br />

Since the demolition <strong>of</strong> these proteins to single amino acids results on loss <strong>of</strong> <strong>coeliac</strong><br />

C<br />

C<br />

N<br />

N<br />

N<br />

TECHNOLOGICAL<br />

PROPERTIES<br />

N N C C C<br />

HMWx HMWy LMW g a<br />

Elasticity & Cohesivity<br />

Extensibility & Viscosity<br />

Fig. 1. Schematic representation <strong>of</strong> gluten protein components. Black segments unique<br />

sequence; white segments repeating sequence; ] intrachain disulphide bond; - interchain<br />

disulphide bond; C C-terminal sequence; N N-terminal sequence; HMWx high-molecular<br />

weight glutenins x-type subunit; HMWy high-molecular weight glutenins y-type subunit;<br />

LMW low-molecular weight glutenins; g-gliadins; a-gliadins.

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