Abstract
Protein extracted from defatted oat (Avena sativa L., variety Sentinel) was acylated with acetic or succinic anhydride at levels of 0.05 and 0.20 g/g protein. Acetic anhydride was more reactive than succinic anhydride in modifying lysine groups. Total essential amino acid content was slightly lowered by acetylation but unaffected by succinylation. Gel filtration chromatography showed some dissociation of oat polypeptides by succinylation. Solubility, emulsifying properties and fat finding capacity were all markedly improved by acylation, and the effect was more pronounced with succinylation. Emulsifying capacity of meat was enhanced by blending with acylated oat protein. Water hydration capacity and foam stability were adversely affected by acylation. Results suggest that acylated oat protein may be a valuable functional ingredient in meat and other emulsion food products.

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