Wheat gluten crosslinking

In previous papers, we have (a) reviewed elimination reactions of disulfide bonds in amino acids, peptides, and proteins under the influence of alkali (5) (b) analyzed factors that may operate during alkali-induced amino acid crosslinking and its prevention (6) (c) demonstrated inhibitory effects of certain amino acids and inorganic anions on lysinoalanine formation during alkali treatment of casein, soy protein, wheat gluten, and wool and on lanthionine formation in wool ( 7, 9) (d) demonstrated that... 

Lysinoalanine formation in casein, lactalbumin, and wheat gluten was measured at 65°C at various pH s for 3 hours. Factors that control the extent of formation of the unnatural amino acid lysinoalanine during food processing and thus the degree of crosslinking in structurally different proteins are discussed. 

VPGVP, which tends to form a type II P turn with proline in position 2 (Fig. 2-24) is present in long tandem repeats e.g., (VPGVG). These extensible regions alternate with short a helices which are crosslinked to other chains. Similar structures are present in silks (Box 2-B) and in proteins of wheat gluten. ... 

Wheat gluten is another protein from plants, which was intensively studied for its material applications. Wheat processing requires the presence of plasticizers such as glycerol or water to disrupt disulfide bonds. To control the formation of a crosslinked network, cysteine, formaldehyde or glutaraldehyde can be added. This contributes also to an improvement in moisture sensitivity and in elongation at break. On the other hand, the wheat gluten fibres have better properties compared to other protein-based bio products for biomedical applications. 

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