Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade proteinglutaminase
(PG), and the effects on structure, solubility and emulsifying properties of oat proteins were
studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins
were deamidated up to a deamidation degree of 59%. The solubility of proteins doubled. Oil-in-water
emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared
from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer
stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure
became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a
promising technique to improve oat protein functionality such as emulsifying ability and solubility