Rheological properties of modified lupin proteins

The properties of acetylated, succinylated and phosphorylated protein isola tes extracted from the flour of yellow lupins (L. luteus) were studied by m eans of oscillatory rheology. The flow behaviour of protein dispersions (15% w/w) and the properties of t hermotropic gels were distinctly influenced by the modification. Succinylat ion increased the viscosity of the dispersions of unmodified protein isolat e (LPI) from 99 mPas to 515 mPas and results in the lowest gel point (T = 3 0.5 degreesC). Acetylation and phosphorylation enhance the pseudoplastic fl ow behaviour of the dispersions. Acylated lupin samples formed the stronges t gels with a small visco-elastic range while phosphorylation leads to weak and "rubber-like" gels.