Abstract
ABSTRACTCorn germ protein isolate (CGPI) was partially hydrolyzed with trypsin and pepsin and succinylated at three levels. Various functional and electrophoretic properties of the native and modified protein were determined. Water absorption and foaming properties of CGPI were Improved by partial hydrolysis with trypsin; emulsifying capacity and nitrogen solubility were reduced; oil absorption was increased only slightly. CGPI pepsin hydrolyzate has decreased oil absorption, nitrogen solubility and emulsifying capacity but improved foaming properties; water absorption was unchanged. Treatment of CGPI with succinic anhydride improved water and oil absorption, nitrogen solubility and foaming capacity but decreased emulsifying capacity; foam stability was unchanged. Succinylation retarded electropohoretic mobility while hydrolysis altered band intensities.
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