Abstract
In this study gliadin solutions were crosslinked with 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride/ N-hydroxysuccinimide (EDC/NHS) and cysteine. The filmogenic solutions were studied through rheological, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and FTIR analysis. Gliadin modified by EDC/NHS showed lower viscosity values when compared with the gliadin/cysteine system and the non-modified gliadin system. Determination of amino groups in gliadin modified by EDC/NHS was carried out through the trinitrobenzenesulfonic acid (TNBS) method. The cast films were evaluated by FTIR analysis in order to detect structural changes in the secondary structure of protein. SDS-PAGE showed the formation of higher protein aggregates, indicating that cysteine promotes gliadin polymerization through covalent bonds (disulfide bonds). The TNBS analysis showed that non-chemically modified gliadin had higher amounts of ε-amino groups when compared with gliadin treated with EDC/NHS; however, both systems revealed similar amounts of amino groups for the whole range of glycerol content. The FTIR spectra for the films showed that the two crosslinking agents act by different mechanisms, promoting changes in the secondary structure of gliadin.
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