Rheological properties of modified lupin proteins

Abstract

The properties of acetylated, succinylated and phosphorylated protein isolates extracted from the flour of yellow lupins (L. luteus) were studied by means of oscillatory rheology. The flow behaviour of protein dispersions (15% w/w) and the properties of thermotropic gels were distinctly influenced by the modification. Succinylation increased the viscosity of the dispersions of unmodified protein isolate (LPI) from 99 mPas to 515 mPas and results in the lowest gel point (T = 30.5 degrees C). Acetylation and phosphorylation enhance the pseudoplastic flow behaviour of the dispersions. Acylated lupin samples formed the strongest gels with a small visco-elastic range while phosphorylation leads to weak and "rubber-like" gels.

Functionality of oilseed protein products: A review

“…Several authors describes as solubility, hydrodynamic properties, hydrophobicity and microstructure of proteins play an important role in the rheological properties of proteins (Krause, Bagger, & Schwenke, 2001;Krase et al, 2002;Paulson & Tung, 1989;Vojdani, 1996). Añ ó n, Sorgentini, and Wagner (2001) suggest that the apparent viscosity of commercial and laboratory soybean isolates depends on interaction between soluble and insoluble proteins which water and between the hydrated particles.…”

Adhesive based on micellar lupin protein isolate exhibiting oxygen barrier properties

“…The storage modulus G ′ is reflecting the elastic component of the protein suspension, while the loss modulus G ″ is characterizing the viscous component. Oscillation measurements can be conducted to determine microstructural differences . These are not only affecting the rheological behavior of suspensions but may give information about interaction of adhesive and substrate, due to changes in surface net charge.…”

“…Oscillation measurements can be conducted to determine microstructural differences. 39,40 These are not only affecting the rheological behavior of suspensions but may give information about interaction of adhesive and substrate, due to changes in (1)]. Minimal particle-particle interactions in a completely Newtonian fluid lead to a d 5 908 while a completely elastic system with maximum interactions shows d 5 08 (Table I).…”

Functional Properties of Soybean Food Ingredients in Food Systems

“…Solubility, hydrodynamic properties, hydrophobicity and microstructure of proteins have been reported to play an important role in the rheological properties of proteins (Krause et al, 2001;Krase et al, 2002). Apparent viscosity of soybean isolates depends on interaction between soluble and insoluble proteins with water and between the hydrated particles (Añón et al, 2001).…”