C. Schorsch et al., Thermodynamic incompatibility and microstructure of milk protein locust bean gum sucrose systems, FOOD HYDROC, 13(2), 1999, pp. 89-99
Phase equilibria of milk protein/locust bean gum systems in high levels of
sucrose were investigated to understand the behaviour of these components i
n diary products and also to look at the particular effect of sucrose. Two
milk protein systems were investigated, skimmed milk (SMP) and native phosp
hocaseinate (PCN). The main advantage of using this latter sample is that i
t is representative of the casein micelles of milk and allows understanding
of what happens in a model system with controlled sugar and salt content.
At a temperature of 5 degrees C, pH 6.8, and at an ionic strength of 0.08 M
, these mixtures tend to phase separate because of high incompatibility. Th
e similarity between the behaviour of SMP/LBG and micellar casein/LBG syste
ms is evident, suggesting that the incompatibility between skimmed milk and
locust bean gum is largely attributable to the incompatibility of micellar
casein and locust bean gum. Ternary phase diagrams, in the absence or pres
ence of 20%, 30% or 40% (w/w) sucrose, were established and compared. Sucro
se has only a slight influence on the thermodynamic compatibility. The addi
tion of sucrose leads to a concentration effect on the protein phase and di
lution of the locust bean gum phase. Some rheological and turbidity measure
ments, as well as observations using confocal laser scanning microscopy and
electron microscopy, were carried out and demonstrated that for the concen
trations, temperatures and times investigated, there is no interaction betw
een the components. The microstructures of mixtures have also been investig
ated in order to study the concentration effect of each biopolymer as well
as the sucrose effect. It was clearly demonstrated that the microstructure
is driven by the phase volume ratio and this probably leads to a difference
in mechanical properties. (C) 1999 Elsevier Science Ltd. All rights reserv
ed.