Enzymatic hydrolysis of defatted wheat germ by proteases and the effect on the functional properties of resulting protein hydrolysates

Endogenous enzymes of wheat germ were inactivated by heating for 15 min at 105C in an oven. The germ was defatted using supercritical carbon dioxide, smashed and solubilized by enzymatic hydrolysis. The enzyme hydrolysate was continuously stirred under conditions of optimum hydrolysis and centrifuged. Defatted wheat germ protein (DWGP) was obtained when the supernatant was spray-dried. The enzymes were used to enhance the solubilization of protein so as to increase the yield of DWGP. Alcalase and flavourzyme (R) solubilized 85 and 80% of the protein, respectively, while papain, neutrase and protamex solubilized 73, 66 and 61%, respectively. The functional properties of DWGP solubilized using alcalase were as follows: nitrogen solubility, 74% at pH 6; emulsifying activity, capacity and stability were 64, 62 and 57%, respectively. Water retention of DWGP solubilized using alcalase was 232% at pH 7 and temperature of 70C. DWGP is a potential source of functional protein for possible food applications.