FUNCTIONAL-PROPERTIES OF ACYLATED FLAX PROTEIN ISOLATES

Flaxseed protein isolates were prepared by sodium hexametaphosphate co mplexation and acylated with acetic or succinic anhydride to improve t heir functional properties. The degree of acylation of free amino grou ps was lower when succinic anhydride was used in place of acetic anhyd ride. The color of the acylated proteins became lighter as the degree of acylation was increased. Emulsification properties of protein prepa rations were improved due to acylation, particularly for succinylated products. While foaming properties of flax protein isolates were not i mproved by acylation, their solubility was markedly improved. Low degr ees of acetylation improved fat binding capacity of flax protein isola tes, but succinylation did not exhibit such an effect. Acylation also increased aromatic or surface hydrophobicity of the products, and the highest value was observed at the lowest degree of acetylation. The in -vitro enzymic hydrolysis of the isolated proteins was reduced due to the acylation process.