Stability and structure of protein-polysaccharide coacervates in the presence of protein aggregates.
We have studied at pH 4.2 and three protein (Pr):polysaccharide (Pol) weight ratios (8:1, 2:1 and 1:1) the structure and stability of beta-lactoglobulin/acacia gum/water dispersions containing protein aggregates (BLG/AG/W) or free from aggregates (AF-BLG/AG/W). Phase diagrams were characteristic of complex coacervation. BLG/AG/W dispersions displayed a larger biphasic area than AF-BLG/AG/W dispersions, that moved towards the protein axis. It was concluded that protein aggregates affected complex coacervation both by entropic (size and molecular masses of aggregates) and enthalpic (surface properties of aggregates) effects. Laser light scattering measurements revealed that the particles diameter (d(43)) induced by demixing was controlled by protein aggregates in AF-BLG/AG/W dispersions. At 1 wt.% biopolymer concentration, particles were 15-20 times larger in AF-BLG/AG/W dispersions than in BLG/AG/W dispersions at (Pr:Pol) ratios of 2:1 or 1:1. Confocal scanning laser microscopy showed that AF-BLG/AG/W dispersions only contained spherical coacervates. BLG/AG/W dispersions contained both coacervates and aggregates coated with AG or/and BLG/AG coacervates. At a (Pr:Pol) ratio of 2:1 and 1:1, coacervates were vesicular or multivesicular. Coacervates were smaller in BLG/AG/W dispersions than in AF-BLG/AG/W dispersions. It was concluded that protein aggregates have the intrinsic ability to stabilize complex coacervates and could be used to design multifunctional delivery systems. This study showed that composite dispersions containing both protein aggregates embedded in protein-polysaccharide coacervates and free coacervates may be performed. In this respect, the design of protein aggregates with controlled size distribution and surface properties could open new possibilities both in the non-chemical control of coacervates stability and in the development of multifunctional delivery systems.
Sanchez
Christian
C
Laboratoire de Physico-Chimie et Génie Alimentaires, ENSAIA-INPL BP 172, 54505 Cedex, Vandoeuvre-les-Nancy, France.
Renard
Denis
D
D004339:Drug Compounding; D004355:Drug Stability; D006170:Gum Arabic; D007782:Lactoglobulins; D018613:Microscopy, Confocal; D008970:Molecular Weight; D010316:Particle Size; D011134:Polysaccharides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D007782:Lactoglobulins; D011134:Polysaccharides; D011506:Proteins; D006170:Gum Arabic