Functional Properties of Deamidated Oat Protein Isolates

ABSTRACT Oat protein isolates were deamidated by mild acid hydrolysis. Amino acid analysis and gel filtraiton chromatography showed no significant cleavage of peptide linkages although the aggregated and oligomeric oat proteins were extensively dissociated. Deamidation led to marked improvement in solubility, emulsifying properties and water and fat binding capacities. The pH for heat‐induced gelation was lowered by deamidation, and a firm, elastic gel was produced by mixing egg white with deamidated oat isolates.