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ABSTRACT

Wheat gliadins, that are glutamine rich and lysine poor proteins, are good substrates for transglutaminases reactions. This study was conducted to determine the efficiency with which guinea pig liver transglutaminase catalyzes transfer and hydrolysis reactions of native and acylated gliadins. In all reactions, 35% of the total glutaminyl residues were modified. Neutral pH simultaneously enhanced glutaminyl residue hydrolysis and protein cross-linking, while acidic pH reduced the cross-linking reaction. Functional properties of two enzymatically modified gliadins and a chemically deamidated one were tested at neutral pH. A deamidation level of 25–27% appeared to be an optimum for the emulsification properties. Enzymatically modified gliadin showed better resistance to coalescence than the chemically deamidated one; a result that probably is related to the presence of high molecular weight polymers.