Preparation and functional properties of a protein isolate from defatted wheat germ

Abstract

A protein isolate (90% protein) was prepared from defatted wheat germ by alkaline extraction at pH 9.5 and isoelectric precipitation at pH 4.0. Nitrogen solubility of wheat germ protein isolate (WGPI) was 72% at pH 6.0. WGPI compared well with bovine serum albumin (BSA) in its emulsifying properties. Foaming capacity of WGPI was similar to that of egg white standard while the foam stability was significantly lower (P 21 kDa MW. Wheat germ offers as a potential source of functional protein isolate for possible food applications.