| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 4562437 | Food Research International | 2009 | 8 Pages |
Oat protein isolate (OPI) was extracted in 0.015 N NaOH and acetylated or succinylated. The thermal analysis of the isolate showed a glass transition (Tg) at 43.4 °C and ΔCp of 0.102 J/g/°C. The positive net charge of OPI and the positive or neutral charge of the modified OPI were apparent from the free capillary zone electrophoresis (FZCE) profiles. Acetylation significantly lowered foaming and emulsifying properties of OPI, while succinylation showed the highest foaming capacity, foam stability, and emulsion stability. Acetylated OPI showed the highest surface hydrophobicity compared to the other samples, while OPI was the most soluble of all. The water holding capacity of all samples analyzed was the same except for acetylated-crosslinked (ACXL). The surface tension test confirmed that unmodified and modified OPI possessed surface activity and the equilibrium surface tensions decreased sharply with increasing protein concentration and leveled off to a constant value. The elastic modulus, G′, for the acetylated OPI suspension exhibited the highest value, while the G′ of the crosslinked (XLOPI) had the lowest. The plateau of G′, was 2961 Pa, 920 Pa, 223 Pa, 41 Pa, and 1.8 Pa for the ACOPI, ACXL, SOPI, and XL, respectively.
